2023
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Artificial cell synthesis using biocatalytic polymerization-induced self-assembly. Belluati A, Jimaja S, Chadwick RJ, Glynn C, Chami M, Happel D, Guo C, Kolmar H, Bruns N. Nat Chem. 2023 Dec 4. doi: 10.1038/s41557-023-01391-y. |
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Cattle-derived knob paratopes grafted onto peripheral loops of the IgG1 Fc region enable the generation of a novel symmetric bispecific antibody format Yanakieva D, Vollmer L, Evers A, Siegmund V, Arras P, Pekar L, Doerner A, Valldorf B, Kolmar H, Zielonka S, Krah S. Front. Immunol. 2023 Oct 24 Vol 14. doi:10.3389/fimmu.2023.1238313 |
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A protein engineering approach towards understanding FKBP51 conformational dynamics and mechanisms of ligand binding. Lerma Romero JA, Meyners C, Rupp N, Hausch F, Kolmar H. Protein Eng Des Sel. 2023 Oct 30:gzad014. doi: 10.1093/protein/gzad014. |
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Penetration of Nanobody-Dextran Polymer Conjugates through Tumor Spheroids. Bitsch P, Baum ES, Beltrán Hernández I, Bitsch S, Harwood J, Oliveira S, Kolmar H. Pharmaceutics. 2023 Sep 22;15(10):2374. doi: 10.3390/pharmaceutics15102374. |
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Conditional activation of an anti-IgM antibody-drug conjugate for precise B cell lymphoma targeting. Schoenfeld K, Harwardt J, Habermann J, Elter A, Kolmar H. Front Immunol. 2023 Sep 28;14:1258700. doi: 10.3389/fimmu.2023.1258700. eCollection 2023. |
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Respiratory syncytial virus-approved mAb Palivizumab as ligand for anti-idiotype nanobody-based synthetic cytokine receptors. Ettich J, Wittich C, Moll JM, Behnke K, Floss DM, Reiners J, Christmann A, Lang PA, Smits SHJ, Kolmar H, Scheller J. J Biol Chem. 2023 Sep 19;299(11):105270. doi: 10.1016/j.jbc.2023.105270. |
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Construction of Semisynthetic Shark vNAR Yeast Surface Display Antibody Libraries. Kolmar H, Grzeschik J, Könning D, Krah S, Zielonka S. Methods Mol Biol. 2023;2702:227-243. doi: 10.1007/978-1-0716-3381-6_11. |
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Generation and engineering of potent single domain antibody-based bispecific IL-18 mimetics resistant to IL-18BP decoy receptor inhibition. Lipinski B, Unmuth L, Arras P, Becker S, Bauer C, Toleikis L, Krah S, Doerner A, Yanakieva D, Boje AS, Klausz K, Peipp M, Siegmund V, Evers A, Kolmar H, Pekar L, Zielonka S. MAbs. 2023 Jan-Dec;15(1):2236265. doi: 10.1080/19420862.2023.2236265. |
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Cell Line Development Using Targeted Gene Integration into MAR-Rich Landing Pads for Stable Expression of Transgenes. Oliviero C, Hinz SC, Grzeschik J, Hock B, Kolmar H, Hagens G. Methods Mol Biol. 2023;2681:343-359. doi: 10.1007/978-1-0716-3279-6_19 |
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Bulk Reformatting of Antibody Fragments Displayed on the Surface of Yeast Cells to Final IgG Format for Mammalian Production. Carrara SC, Bogen JP, Fiebig D, Grzeschik J, Hock B, Kolmar H. Methods Mol Biol. 2023;2681:291-311. doi: 10.1007/978-1-0716-3279-6_16. |
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Accessing Transient Binding Pockets by Protein Engineering and Yeast Surface Display Screening. Lerma Romero JA, Kolmar H. Methods Mol Biol. 2023;2681:249-274. doi: 10.1007/978-1-0716-3279-6_14. |
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One-Pot Droplet RT-OE-PCR for the Generation of Natively Paired Antibody Immune Libraries. Yanakieva D, Vollmer L, Kumar S, Becker S, Toleikis L, Pekar L, Kolmar H, Zielonka S, Krah S. Methods Mol Biol. 2023;2681:213-229. doi: 10.1007/978-1-0716-3279-6_12. |
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Isolation of Antigen-Specific Unconventional Bovine Ultra-Long CDR3H Antibodies Using Cattle Immunization in Combination with Yeast Surface Display. Arras P, Zimmermann J, Lipinski B, Yanakieva D, Klewinghaus D, Krah S, Kolmar H, Pekar L, Zielonka S. Methods Mol Biol. 2023;2681:113-129. doi: 10.1007/978-1-0716-3279-6_8. |
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Characterization of lipoprotein supplement and influence of its oxidized lipid content on cell culture performance and monoclonal antibody production by a SP2/0 hybridoma cell line. Moisant R, Cowles E, Broutel L, Deparis V, Baud A, von Hagen J, Kolmar H. Biotechnol Prog. 2023 Sep-Oct;39(5):e3372. doi: 10.1002/btpr.3372. Epub 2023 Jun 27. |
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Novel amino-Li resin for water-based solid-phase peptide synthesis. Uth C, Englert S, Avrutina O, Kolmar H, Knauer S. J Pept Sci. 2023 Jun 15:e3527. doi: 10.1002/psc.3527. |
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Generation of a symmetrical trispecific NK cell engager based on a two-in-one antibody. Harwardt J, Carrara SC, Bogen JP, Schoenfeld K, Grzeschik J, Hock B, Kolmar H. Front Immunol. 2023 Apr 4;14:1170042. doi: 10.3389/fimmu.2023.1170042. eCollection 2023. |
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Parahydrogen-induced polarization allows 2000-fold signal enhancement in biologically active derivatives of the peptide-based drug octreotide. Lins J, Miloslavina YA, Carrara SC, Rösler L, Hofmann S, Herr K, Theiß F, Wienands L, Avrutina O, Kolmar H, Buntkowsky G. |
2022
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Targeted Phagocytosis Induction for Cancer Immunotherapy via Bispecific MerTK-Engaging Antibodies. Carrara SC, Bogen JP, Fiebig D, Grzeschik J, Hock B, Kolmar H. Int J Mol Sci. 2022 Dec 10;23(24):15673. doi: 10.3390/ijms232415673. |
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Tag-free, specific conjugation of glycosylated IgG1 antibodies using microbial transglutaminase Hadjabdelhafid-Parisien A, Bitsch S, Macarrón Palacios A, Deweid L, Kolmar H, Pelletier JN. RSC Adv., 2022, 12, 33510-33515. DOI: 10.1039/D2RA05630E (Paper) |
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TriTECM: A tetrafunctional T-cell engaging antibody with built-in risk mitigation of cytokine release syndrome Carrara S, Harwardt J, Grzeschik J, Hock B, Kolmar H. Front. Immunol., 10 November 2022 Sec. Vaccines and Molecular Therapeutics https://doi.org/10.3389/fimmu.2022.1051875 |
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Beyond bispecificity: Controlled Fab arm exchange for the generation of antibodies with multiple specificities. Yanakieva D, Pekar L, Evers A, Fleischer M, Keller S, Mueller-Pompalla D, Toleikis L, Kolmar H, Zielonka S, Krah S. MAbs. 2022 Jan-Dec;14(1):2018960. doi: 10.1080/19420862.2021.2018960 |
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Grabbing the Bull by Both Horns: Bovine Ultralong CDR-H3 Paratopes Enable Engineering of ‘Almost Natural’ Common Light Chain Bispecific Antibodies Suitable For Effector Cell Redirection. Klewinghaus D, Pekar L, Arras P, Krah S, Valldorf B, Kolmar H, Zielonka S. Frontiers in Immunology, January 2022, Volume 12,Article 801368. doi: doi.org/10.3389/fimmu.2021.801368. Binding pocket stabilization by high-throughput screening of yeast display libraries. Lerma Romero JA, Meyners C, Christmann A, Reinbold LM, Charalampidou A, Hausch F, Kolmar H. Front Mol Biosci. 2022 Nov 7;9:1023131. doi: 10.3389/fmolb.2022.1023131. eCollection 2022. PMID: 36419931 |
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Sactipeptide Engineering by Probing the Substrate Tolerance of a Thioether-Bond-Forming Sactisynthase. Ali A, Happel D, Habermann J, Schoenfeld K, Macarrón Palacios A, Bitsch S, Englert S, Schneider H, Avrutina O, Fabritz S, Kolmar H. Angew Chem Int Ed Engl. 2022 Nov 7;61(45):e202210883. doi: 10.1002/anie.202210883. Epub 2022 Oct 12. |
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Triplet States Reveal Slow Local Dynamics in the Solvation Shell of Biomolecules. Weigl P, Weißheit S, Pabst F, Kolmar H, Thiele CM, Walther T, Blochowicz T. J Phys Chem B. 2022 Aug 25;126(33):6324-6330. doi:10.1021/acs.jpcb.2c03784. Epub 2022 Aug 16. |
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Carotenoids in Human SkinIn Vivo: Antioxidant and Photo-Protectant Role against External and Internal Stressors. Darvin ME, Lademann J, von Hagen J, Lohan SB, Kolmar H, Meinke MC, Jung S. Antioxidants (Basel). 2022 Jul 26;11(8):1451. doi:10.3390/antiox11081451. |
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Engineering of ultraID, a compact and hyperactive enzyme for proximity-dependent biotinylation in living cells. Kubitz L, Bitsch S, Zhao X, Schmitt K, Deweid L, Roehrig A, Barazzone EC, Valerius O, Kolmar H, Béthune J. Commun Biol. 2022 Jul 4;5(1):657. doi: 10.1038/s42003-022-03604-5. |
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Streamlining the Transition From Yeast Surface Display of Antibody Fragment Immune Libraries to the Production as IgG Format in Mammalian Cells. Fiebig D, Bogen JP, Carrara SC, Deweid L, Zielonka S, Grzeschik J, Hock B, Kolmar H. Front Bioeng Biotechnol. 2022 May 10;10:794389. doi: 10.3389/fbioe.2022.794389. eCollection 2022. |
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Humanization of Chicken-Derived Antibodies by Yeast Surface Display. Bogen JP, Elter A, Grzeschik J, Hock B, Kolmar H. Methods Mol Biol. 2022;2491:335-360. doi: 10.1007/978-1-0716-2285-8_18. |
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Antibody Library Screening Using Yeast Biopanning and Fluorescence-Activated Cell Sorting. Carrara SC, Bogen JP, Grzeschik J, Hock B, Kolmar H. Methods Mol Biol. 2022;2491:177-193. doi: 10.1007/978-1-0716-2285-8_10. |
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A Generic Strategy to Generate Bifunctional Two-in-One Antibodies by Chicken Immunization. Harwardt J, Bogen JP, Carrara SC, Ulitzka M, Grzeschik J, Hock B, Kolmar H. Front Immunol. 2022 Apr 11;13:888838. doi: 10.3389/fimmu.2022.888838. eCollection 2022. |
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Generation of a host cell line containing a MAR-rich landing pad for site-specific integration and expression of transgenes. Oliviero C, Hinz SC, Bogen JP, Kornmann H, Hock B, Kolmar H, Hagens G. Biotechnol Prog. 2022 Jul;38(4):e3254. doi: 10.1002/btpr.3254. Epub 2022 Apr 25. |
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Lateral Dermal Penetration Is Dependent on the Lipophilicity of Active Ingredients. Lubda M, Zander M, Salazar A, Kolmar H, von Hagen J. Skin Pharmacol Physiol. 2022;35(4):235-246. doi: 10.1159/000522633. Epub 2022 Feb 16. |
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Treating Bladder Cancer: Engineering of Current and Next Generation Antibody-, Fusion Protein-, mRNA-, Cell- and Viral-Based Therapeutics. Bogen JP, Grzeschik J, Jakobsen J, Bähre A, Hock B, Kolmar H. Front Oncol. 2021 May 27;11:672262. doi: 10.3389/fonc.2021.672262. eCollection 2021. PMID: 34123841 |
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Synthetic Integrin-Targeting Dextran-Fc Hybrids Efficiently Inhibit Tumor Proliferation In Vitro. Schneider H, Englert S, Macarrón Palacios A, Lerma Romero JA, Ali A, Avrutina O, Kolmar H. Front Chem. 2021 Jul 22;9:693097. doi: 10.3389/fchem.2021.693097. eCollection 2021. PMID: 34368077 |
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Vom Huhn abgeleitete Antikörper für Diagnostik und Immuntherapie. Elter A, Bogen JP, Habermann J, Kolmar H. Biospektrum (Heidelb). 2021;27(5):500-504. doi: 10.1007/s12268-021-1623-3. Epub 2021 Sep 4. PMID: 34511735 |
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EGFR binding Fc domain-drug conjugates: stable and highly potent cytotoxic molecules mediate selective cell killing. Jäger S, Dickgiesser S, Tonillo J, Hecht S, Kolmar H, Schröter C. Biol Chem. 2021 Sep 20. doi: 10.1515/hsz-2021-0321. PMID: 34535048 |
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Milking the Cow: Cattle-Derived Chimeric Ultralong CDR-H3 Antibodies and Their Engineered CDR-H3-Only Knobbody Counterparts Targeting Epidermal Growth Factor Receptor Elicit Potent NK Cell-Mediated Cytotoxicity. Pekar L, Klewinghaus D, Arras P, Carrara SC, Harwardt J, Krah S, Yanakieva D, Toleikis L, Smider VV, Kolmar H, Zielonka S. Front Immunol. 2021 Oct 25;12:742418. doi: 10.3389/fimmu.2021.742418. eCollection 2021. PMID: 34759924 |
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Methoxy-Monobenzoylmethane Protects Skin from UV-Induced Damages in a Randomized, Placebo Controlled, Double-Blinded Human In Vivo Study and Prevents Signs of Inflammation While Improving the Skin Barrier. Termer M, Jaeger A, Carola C, Salazar A, Keck CM, Kolmar H, von Hagen J. Dermatol Ther (Heidelb). 2021 Dec 22. doi: 10.1007/s13555-021-00652-3. PMID: 34939179 |
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Native llama Nanobody Library Panning Performed by Phage and Yeast Display Provides Binders Suitable for C-Reactive Protein Detection. Oloketuyi S, Bernedo R, Christmann A, Borkowska J, Cazzaniga G, Schuchmann HW, Niedziółka-Jönsson J, Szot-Karpińska K, Kolmar H, de Marco A. Biosensors (Basel). 2021 Dec 3;11(12):496. doi: 10.3390/bios11120496. PMID: 34940253 |
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Effect of conjugation site and technique on the stability and pharmacokinetics of antibody-drug conjugates. Kaempffe A, Dickgiesser S, Rasche N, Paoletti A, Bertotti E, De Salve I, Sirtori FR, Kellner R, Könning D, Hecht S, Anderl J, Kolmar H, Schröter C. J Pharm Sci. 2021 Aug 4:S0022-3549(21)00400-7. doi: 10.1016/j.xphs.2021.08.002. PMID: 34363839 |
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Protease-Activation of Fc-Masked Therapeutic Antibodies to Alleviate Off-Tumor Cytotoxicity Elter A, Yanakieva S, Fiebig D, Hallstein K, Becker S, Betz U, Kolmar H. Front. Immunol., 03 August 2021 | https://doi.org/10.3389/fimmu.2021.715719 |
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Generation and Biological Evaluation of Fc Antigen Binding Fragment-Drug Conjugates as a Novel Antibody-Based Format for Targeted Drug Delivery. Jäger S, Wagner TR, Rasche N, Kolmar H, Hecht S, Schröter C. Bioconjug Chem. 2021 Jun 29. doi: 10.1021/acs.bioconjchem.1c00240. Online ahead of print. PMID: 34185508 |
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Use of 5-Thio-L-Fucose to modulate binding affinity of therapeutic proteins. Zimmermann M, Nguyen M, Schultheiss CM, Kolmar H, Zimmer A. Biotechnol Bioeng. 2021 Jan 27. doi: 10.1002/bit.27695. |
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Design of a Trispecific Checkpoint Inhibitor and Natural Killer Cell Engager Based on a 2 + 1 Common Light Chain Antibody Architecture. Bogen JP, Carrara SC, Fiebig D, Grzeschik J, Hock B, Kolmar H. Front Immunol. 2021 May 10;12:669496. doi: 10.3389/fimmu.2021.669496. eCollection 2021. PMID: 34040611 |
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Recombinant Antibody Production Using a Dual-Promoter Single Plasmid System. Carrara SC, Fiebig D, Bogen JP, Grzeschik J, Hock B, Kolmar H. Antibodies (Basel). 2021 May 13;10(2):18. doi: 10.3390/antib10020018. PMID: 34068440 |
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Use of 5-Thio-L-Fucose to modulate binding affinity of therapeutic proteins. Zimmermann M, Nguyen M, Schultheiss CM, Kolmar H, Zimmer A. Biotechnol Bioeng. 2021 Jan 27. doi: 10.1002/bit.27695. |
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S-Sulfocysteine – Investigation of cellular uptake in CHO cells. Zimmermann M, Kolmar H, Zimmer A. J Biotechnol. 2021 Jul 20;335:27-38. doi: 10.1016/j.jbiotec.2021.06.003. Epub 2021 Jun 4. PMID: 34090949 |
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Toward Fabrication of Bioactive Papers: Covalent Immobilization of Peptides and Proteins. Liebich VJ, Avrutina O, Habermann J, Hillscher LM, Langhans M, Meckel T, Biesalski M, Kolmar H. Biomacromolecules. 2021 Jun 8. doi: 10.1021/acs.biomac.1c00354. Online ahead of print. PMID: 34101458 |
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Carbohydrate binding module-fused antibodies improve the performance of cellulose-based lateral flow immunoassays. Elter A, Bock T, Spiehl D, Russo G, Hinz SC, Bitsch S, Baum E, Langhans M, Meckel T, Dörsam E, Kolmar H, Schwall G. Sci Rep. 2021 Apr 12;11(1):7880. doi: 10.1038/s41598-021-87072-7. PMID: 33846482 |
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Isolation of Common Light Chain Antibodies from Immunized Chickens Using Yeast Biopanning and Fluorescence-Activated Cell Sorting. Bogen JP, Storka J, Yanakieva D, Fiebig D, Grzeschik J, Hock B, Kolmar H. Biotechnol J. 2021 Mar;16(3):e2000240. doi: 10.1002/biot.202000240. Epub 2020 Oct 8. PMID: 32914549 |
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Functional paper-based materials for diagnostics. Hillscher LM, Liebich VJ, Avrutina O, Biesalski M, Kolmar H. ChemTexts. 2021;7(2):14. doi: 10.1007/s40828-021-00139-w. Epub 2021 Mar 31. PMID: 33816066 |
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Humanization of Chicken-Derived scFv Using Yeast Surface Display and NGS Data Mining. Elter A, Bogen JP, Hinz SC, Fiebig D, Macarrón Palacios A, Grzeschik J, Hock B, Kolmar H. Biotechnol J. 2021 Mar;16(3):e2000231. doi: 10.1002/biot.202000231. Epub 2020 Nov 9. PMID: 33078896 |
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From cell line development to the formulated drug product: The art of manufacturing therapeutic monoclonal antibodies. Carrara SC, Ulitzka M, Grzeschik J, Kornmann H, Hock B, Kolmar H. Int J Pharm. 2021 Feb 1;594:120164. doi: 10.1016/j.ijpharm.2020.120164. |
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Affinity Maturation of B7-H6 Translates into Enhanced NK Cell-Mediated Tumor Cell Lysis and Improved Proinflammatory Cytokine Release of Bispecific Immunoligands via NKp30 Engagement. Pekar L, Klausz K, Busch M, Valldorf B, Kolmar H, Wesch D, Oberg HH, Krohn S, Boje AS, Gehlert CL, Toleikis L, Krah S, Gupta T, Rabinovich B, Zielonka S, Peipp M. J Immunol. 2021 Jan 1;206(1):225-236. doi: 10.4049/jimmunol.2001004. |
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Multivalent dextran hybrids for efficient cytosolic delivery of biomolecular cargoes. Becker B, Englert S, Schneider H, Yanakieva D, Hofmann S, Dombrowsky C, Macarrón Palacios A, Bitsch S, Elter A, Meckel T, Kugler B, Schirmacher A, Avrutina O, Diederichsen U, Kolmar H. J Pept Sci. 2021 Jan 17:e3298. doi: 10.1002/psc.3298. |
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Enhancing the Pharmacokinetics and Antitumor Activity of an α-Amanitin-Based Small-Molecule Drug Conjugate via Conjugation with an Fc Domain. Gallo F, Korsak B, Müller C, Hechler T, Yanakieva D, Avrutina O, Kolmar H, Pahl A. J Med Chem. 2021 Mar 23. doi: 10.1021/acs.jmedchem.1c00003. Online ahead of print. PMID: 33755471 |
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Comparison of Membrane Depth Determination Techniques for Active Ingredient Skin Penetration Studies Using Microdialysis. Lubda M, Zander M, Salazar A, Kolmar H, von Hagen J. Skin Pharmacol Physiol. 2021 May 21:1-11. doi: 10.1159/000515113. |
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Solvent-Containing Closure Material Can Be Used to Prevent Follicular Penetration of Caffeine and Fluorescein Sodium Salt on Porcine Ear Skin. Klein AL, Lubda M, Akbarzadeh Taghavi P, Lademann J, Beckers I, von Hagen J, Kolmar H, Patzelt A. Skin Pharmacol Physiol. 2020;33(2):117-126. doi: 10.1159/000505839. |
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Characterization of soy protein hydrolysates and influence of its iron content on monoclonal antibody production by a murine hybridoma cell line. Djemal L, von Hagen J, Kolmar H, Deparis V. Biotechnol Prog. 2021 Mar 20:e3147. doi: 10.1002/btpr.3147. Online ahead of print. PMID: 33742790 |
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Review: High temperature short time treatment of cell culture media and feed solutions to mitigate adventitious viral contamination in the biopharmaceutical industry. Djemal L, Fournier C, von Hagen J, Kolmar H, Deparis V. Biotechnol Prog. 2021 May;37(3):e3117. doi: 10.1002/btpr.3117. Epub 2021 Jan 9. PMID: 33372404 |
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A Generic Procedure for the Isolation of pH- and Magnesium-Responsive Chicken scFvs for Downstream Purification of Human Antibodies. Hinz SC, Elter A, Rammo O, Schwämmle A, Ali A, Zielonka S, Herget T, Kolmar H. Front Bioeng Biotechnol. 2020 Jun 23;8:688. doi: 10.3389/fbioe.2020.00688. eCollection 2020. |
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Isolation of Common Light Chain Antibodies from Immunized Chickens Using Yeast Biopanning and Fluorescence-Activated Cell Sorting. Bogen JP, Storka J, Yanakieva D, Fiebig D, Grzeschik J, Hock B, Kolmar H. Biotechnol J. 2020 Sep 10:e2000240. doi: 10.1002/biot.202000240. |
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Dissecting capture and twisting of aureolysin and pseudolysin: functional amino acids of the Dispase autolysis-inducing protein. Fiebig D, Anderl A, Al Djaizani S, Kolmar H, Fuchsbauer HL. Biochem J. 2020 Jul 17;477(13):2595-2606. doi: 10.1042/BCJ20200407. |
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Expeditious Generation of Biparatopic Common Light Chain Antibodies via Chicken Immunization and Yeast Display Screening. Bogen JP, Carrara SC, Fiebig D, Grzeschik J, Hock B, Kolmar H. Front Immunol. 2020 Dec 23;11:606878. doi: 10.3389/fimmu.2020.606878. eCollection 2020. |
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FACS-Based Functional Protein Screening via Microfluidic Co-encapsulation of Yeast Secretor and Mammalian Reporter Cells. Yanakieva D, Elter A, Bratsch J, Friedrich K, Becker S, Kolmar H. Sci Rep. 2020 Jun 23;10(1):10182. doi: 10.1038/s41598-020-66927-5. |
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A Bioorthogonal Click Chemistry Toolbox for Targeted Synthesis of Branched and Well-Defined Protein-Protein Conjugates. Baalmann M, Neises L, Bitsch S, Schneider H, Deweid L, Werther P, Ilkenhans N, Wolfring M, Ziegler MJ, Wilhelm J, Kolmar H, Wombacher R. Angew Chem Int Ed Engl. 2020 Jul 27;59(31):12885-12893. doi: 10.1002/anie.201915079. |
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Humanization of Chicken-Derived scFv Using Yeast Surface Display and NGS Data Mining. Elter A, Bogen JP, Hinz SC, Fiebig D, Macarrón Palacios A, Grzeschik J, Hock B, Kolmar H. Biotechnol J. 2020 Oct 20:e2000231. doi: 10.1002/biot.202000231. |
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Review: High temperature short time treatment of cell culture media and feed solutions to mitigate adventitious viral contamination in the biopharmaceutical industry. Djemal L, Fournier C, von Hagen J, Kolmar H, Deparis V. Biotechnol Prog. 2020 Dec 28:e3117. doi: 10.1002/btpr.3117. |
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Specific Targeting of Lymphoma Cells Using Semisynthetic Anti-Idiotype Shark Antibodies. Macarrón Palacios A, Grzeschik J, Deweid L, Krah S, Zielonka S, Rösner T, Peipp M, Valerius T, Kolmar H. Front Immunol. 2020 Nov 26;11:560244. doi: 10.3389/fimmu.2020.560244. eCollection 2020. |
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From cell line development to the formulated drug product: The art of manufacturing therapeutic monoclonal antibodies. Carrara SC, Ulitzka M, Grzeschik J, Kornmann H, Hock B, Kolmar H. Int J Pharm. 2021 Feb 1;594:120164. doi: 10.1016/j.ijpharm.2020.120164. Epub 2020 Dec 10. |
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Engineering therapeutic antibodies for patient safety: tackling the immunogenicity problem. Ulitzka M, Carrara S, Grzeschik J, Kornmann H, Hock B, Kolmar H. Protein Eng Des Sel. 2020 Sep 14;33:gzaa025. doi: 10.1093/protein/gzaa025. |
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Glutamine-walking: Creating reactive substrates for transglutaminase-mediated protein labeling. Deweid L, Hadjabdelhafid-Parisien A, Lafontaine K, Rochet LNC, Kolmar H, Pelletier JN. Methods Enzymol. 2020;644:121-148. doi: 10.1016/bs.mie.2020.04.066. Epub 2020 May 20. |
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Sustainable Peptide Synthesis Enabled by a Transient Protecting Group. Knauer S, Koch N, Uth C, Meusinger R, Avrutina O, Kolmar H. Angew Chem Int Ed Engl. 2020 Jul 27;59(31):12984-12990. doi: 10.1002/anie.202003676. Epub 2020 May 29. |
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Intein mediated high throughput screening for bispecific antibodies. Hofmann T, Schmidt J, Ciesielski E, Becker S, Rysiok T, Schütte M, Toleikis L, Kolmar H, Doerner A. MAbs. 2020 Jan-Dec;12(1):1731938. doi: 10.1080/19420862.2020.1731938. |
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Solvent-Containing Closure Material Can Be Used to Prevent Follicular Penetration of Caffeine and Fluorescein Sodium Salt on Porcine Ear Skin. Klein AL, Lubda M, Akbarzadeh Taghavi P, Lademann J, Beckers I, von Hagen J, Kolmar H, Patzelt A. Skin Pharmacol Physiol. 2020 Feb 11:1-9. doi: 10.1159/000505839. [Epub ahead of print] |
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Recent progress in transglutaminase-mediated assembly of antibody-drug conjugates. Schneider H, Deweid L, Avrutina O, Kolmar H. Anal Biochem. 2020 Apr 15;595:113615. doi: 10.1016/j.ab.2020.113615. Epub 2020 Feb 5. Review. |
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The metal-binding properties of the long chaplin from Streptomyces mobaraensis: A bioinformatic and biochemical approach. Anderl A, Kolmar H, Fuchsbauer HL. J Inorg Biochem. 2020 Jan;202:110878. doi: 10.1016/j.jinorgbio.2019.110878. Epub 2019 Oct 21. |
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Rapid Generation of Chicken Immune Libraries for Yeast Surface Display. Bogen JP, Grzeschik J, Krah S, Zielonka S, Kolmar H. Methods Mol Biol. 2020;2070:289-302. doi: 10.1007/978-1-4939-9853-1_16. |
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Isolation of Anti-Hapten Antibodies by Fluorescence-Activated Cell Sorting of Yeast-Displayed B-Cell Receptor Gene Repertoires. Jäger S, Krah S, Könning D, Rosskopf J, Dickgiesser S, Rasche N, Kolmar H, Hecht S, Schröter C. Methods Mol Biol. 2020;2070:267-287. doi: 10.1007/978-1-4939-9853-1_15. |
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Isolation of Tailor-Made Antibody Fragments from Yeast-Displayed B-Cell Receptor Repertoires by Multiparameter Fluorescence-Activated Cell Sorting. Kaempffe A, Jäger S, Könning D, Kolmar H, Schröter C. Methods Mol Biol. 2020;2070:249-266. doi: 10.1007/978-1-4939-9853-1_14. |
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Simplifying the Detection of Surface Presentation Levels in Yeast Surface Display by Intracellular tGFP Expression. Hinz SC, Elter A, Grzeschik J, Habermann J, Becker B, Kolmar H. Methods Mol Biol. 2020;2070:211-222. doi: 10.1007/978-1-4939-9853-1_12. |
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Selection and Characterization of Anti-idiotypic Shark Antibody Domains. Könning D, Zielonka S, Kaempffe A, Jäger S, Kolmar H, Schröter C. Methods Mol Biol. 2020;2070:191-209. doi: 10.1007/978-1-4939-9853-1_11. |
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Protein engineering comes of age. Kolmar H. Biol Chem. 2019 Feb 25;400(3):255-256. doi: 10.1515/hsz-2019-0108. |
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Efficient Site-Specific Antibody-Drug Conjugation by Engineering of a Nature-Derived Recognition Tag for Microbial Transglutaminase. Ebenig A, Juettner NE, Deweid L, Avrutina O, Fuchsbauer HL, Kolmar H. Chembiochem. 2019 May 2. doi: 10.1002/cbic.201900101. |
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Biochemical study of sortase E2 from Streptomyces mobaraensis and determination of transglutaminase cross-linking sites. Anderl A, Ferlemann C, Muth M, Henkel-Gupalo A, Ebenig A, Brenner-Weiß G, Kolmar H, Fuchsbauer HL. FEBS Lett. 2019 Jun 3. doi: 10.1002/1873-3468.13466. |
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Tailoring Activity and Selectivity of Microbial Transglutaminase Lukas Deweid, Olga Avrutina, Harald Kolmar Methods Mol Biol. 2019;2012:151-169. doi: 10.1007/978-1-4939-9546-2_9. |
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Site-Specific Antibody–Drug Conjugation Using Microbial Transglutaminase Stephan Dickgiesser, Lukas Deweid, Roland Kellner, Harald Kolmar, Nicolas Rasche Methods Mol Biol. 2019;2012:135-149. doi: 10.1007/978-1-4939-9546-2_8. |
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SpyLigase-Catalyzed Modification of Antibodies Vanessa Siegmund, Birgit Piater, Frank Fischer, Harald Kolmar Methods Mol Biol. 2019;2012:171-192. doi: 10.1007/978-1-4939-9546-2_10. |
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Dextramabs: A Novel Format of Antibody-Drug Conjugates Featuring a Multivalent Polysaccharide Scaffold. Schneider H, Deweid L, Pirzer T, Yanakieva D, Englert S, Becker B, Avrutina O, Kolmar H. ChemistryOpen. 2019 Mar 28;8(3):354-357. |
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Ultrafast Single-Scan 2D NMR Spectroscopic Detection of a PHIP-Hyperpolarized Protease Inhibitor. Kiryutin AS, Sauer G, Tietze D, Brodrecht M, Knecht S, Yurkovskaya AV, Ivanov KL, Avrutina O, Kolmar H, Buntkowsky G. Chemistry. 2019 Mar 15;25(16):4025-4030. |
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A tightly regulated and adjustable CRISPR-dCas9 based AND gate in yeast. Hofmann A, Falk J, Prangemeier T, Happel D, Köber A, Christmann A, Koeppl H, Kolmar H. Nucleic Acids Res. 2019 Jan 10;47(1):509-520. |
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Facile generation of antibody heavy and light chain diversities for yeast surface display by Golden Gate Cloning. Roth L, Grzeschik J, Hinz SC, Becker S, Toleikis L, Busch M, Kolmar H, Krah S, Zielonka S. Biol Chem. 2019 Feb 25;400(3):383-393. |
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Light-Controlled Chemoenzymatic Immobilization of Proteins towards Engineering of Bioactive Papers. Hilberg V, Avrutina O, Ebenig A, Yanakieva D, Meckel T, Biesalski M, Kolmar H. Chemistry. 2019 Feb 1;25(7):1746-1751. |
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Microbial transglutaminase for biotechnological and biomedical engineering. Deweid L, Avrutina O, Kolmar H. Biol Chem. 2019 Feb 25;400(3):257-274. |
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Yeast Surface Display in Combination with Fluorescence-activated Cell Sorting Enables the Rapid Isolation of Antibody Fragments Derived from Immunized Chickens. Grzeschik J, Yanakieva D, Roth L, Krah S, Hinz SC, Elter A, Zollmann T, Schwall G, Zielonka S, Kolmar H. Biotechnol J. 2019 Apr;14(4):e1800466. |
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The metal-binding properties of the long chaplin from Streptomyces mobaraensis: A bioinformatic and biochemical approach. Anderl A, Kolmar H, Fuchsbauer HL. J Inorg Biochem. 2019 Oct 21;202:110878. |
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Rapid Generation of Chicken Immune Libraries for Yeast Surface Display. Bogen JP, Grzeschik J, Krah S, Zielonka S, Kolmar H. Methods Mol Biol. 2020;2070:289-302. |
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Isolation of Anti-Hapten Antibodies by Fluorescence-Activated Cell Sorting of Yeast-Displayed B-Cell Receptor Gene Repertoires. Jäger S, Krah S, Könning D, Rosskopf J, Dickgiesser S, Rasche N, Kolmar H, Hecht S, Schröter C. Methods Mol Biol. 2020;2070:267-287. |
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Isolation of Tailor-Made Antibody Fragments from Yeast-Displayed B-Cell Receptor Repertoires by Multiparameter Fluorescence-Activated Cell Sorting. Kaempffe A, Jäger S, Könning D, Kolmar H, Schröter C. Methods Mol Biol. 2020;2070:249-266 |
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Simplifying the Detection of Surface Presentation Levels in Yeast Surface Display by Intracellular tGFP Expression. Hinz SC, Elter A, Grzeschik J, Habermann J, Becker B, Kolmar H. Methods Mol Biol. 2020;2070:211-222 |
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Selection and Characterization of Anti-idiotypic Shark Antibody Domains. Könning D, Zielonka S, Kaempffe A, Jäger S, Kolmar H, Schröter C. Methods Mol Biol. 2020;2070:191-209. |
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Dual Function pH Responsive Bispecific Antibodies for Tumor Targeting and Antigen Depletion in Plasma. Bogen JP, Hinz SC, Grzeschik J, Ebenig A, Krah S, Zielonka S, Kolmar H. Front Immunol. 2019 Aug 9;10:1892. |
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TRAIL-Inspired Multivalent Dextran Conjugates Efficiently Induce Apoptosis upon DR5 Receptor Clustering. Schneider H, Yanakieva D, Macarrón A, Deweid L, Becker B, Englert S, Avrutina O, Kolmar H. Chembiochem. 2019 Jun 17 |
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Generation of Semi-Synthetic Shark IgNAR Single-Domain Antibody Libraries. Grzeschik J, Könning D, Hinz SC, Krah S, Schröter C, Empting M, Kolmar H, Zielonka S. Methods Mol Biol. 2018;1701:147-167. doi: 10.1007/978-1-4939-7447-4_8. |
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Selection of Antibodies with Tailored Properties by Application of High-Throughput Multiparameter Fluorescence-Activated Cell Sorting of Yeast-Displayed Immune Libraries. Schröter C, Beck J, Krah S, Zielonka S, Doerner A, Rhiel L, Günther R, Toleikis L, Kolmar H, Hock B, Becker S. Mol Biotechnol. 2018 Oct;60(10):727-735. doi: 10.1007/s12033-018-0109-0. |
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Destructive twisting of neutral metalloproteases: the catalysis mechanism of the Dispase autolysis-inducing protein from Streptomyces mobaraensis DSM 40487. Fiebig D, Storka J, Roeder M, Meyners C, Schmelz S, Blankenfeldt W, Scrima A, Kolmar H, Fuchsbauer HL. FEBS J. 2018 Nov;285(22):4246-4264. doi: 10.1111/febs.14647. |
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Construction of Histidine-Enriched Shark IgNAR Variable Domain Antibody Libraries for the Isolation of pH-Sensitive vNAR Fragments. Könning D, Hinz S, Grzeschik J, Schröter C, Krah S, Zielonka S, Kolmar H. Methods Mol Biol. 2018;1827:109-127. doi: 10.1007/978-1-4939-8648-4_6. |
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A Streamlined Approach for the Construction of Large Yeast Surface Display Fab Antibody Libraries. Krah S, Grzeschik J, Rosowski S, Gaa R, Willenbuecher I, Demir D, Toleikis L, Kolmar H, Becker S, Zielonka S. Methods Mol Biol. 2018;1827:145-161. doi: 10.1007/978-1-4939-8648-4_8. |
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Structure of a glutamine donor mimicking inhibitory peptide shaped by the catalytic cleft of microbial transglutaminase. Juettner NE, Schmelz S, Kraemer A, Knapp S, Becker B, Kolmar H, Scrima A, Fuchsbauer HL. FEBS J. 2018 Dec;285(24):4684-4694. doi: 10.1111/febs.14678. |
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Yeast Surface Display in Combination with Fluorescence-activated Cell Sorting Enables the Rapid Isolation of Antibody Fragments Derived from Immunized Chickens. Grzeschik J, Yanakieva D, Roth L, Krah S, Hinz SC, Elter A, Zollmann T, Schwall G, Zielonka S, Kolmar H. Biotechnol J. 2019 Apr;14(4):e1800466. doi: 10.1002/biot.201800466. |
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A novel one-step approach for the construction of yeast surface display Fab antibody libraries. Rosowski S, Becker S, Toleikis L, Valldorf B, Grzeschik J, Demir D, Willenbücher I, Gaa R, Kolmar H, Zielonka S, Krah S. Microb Cell Fact. 2018 Jan 9;17(1):3. doi: 10.1186/s12934-017-0853-z. |
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Beyond antibody engineering: directed evolution of alternative binding scaffolds and enzymes using yeast surface display. Könning D, Kolmar H. Microb Cell Fact. 2018 Feb 26;17(1):32. doi: 10.1186/s12934-018-0881-3. Review. |
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Shark attack: Haiantikörper für Biomedizin und Biotechnologie. D Könning, J Grzeschik, SC Hinz, S Krah, M Empting, H Kolmar, S. Zielonka BIOspektrum, March 2018, Volume 24, Issue 2, pp 142–145 |
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Covalent Attachment of Enzymes to Paper Fibers for Paper-Based Analytical Devices. Böhm A, Trosien S, Avrutina O, Kolmar H, Biesalski M. Front. Chem. | doi: 10.3389/fchem.2018.00214 |
| Isolation of pH-Sensitive Antibody Fragments by Fluorescence-Activated Cell Sorting and Yeast Surface Display. Schröter C, Krah S, Beck J, Könning D, Grzeschik J, Valldorf B, Zielonka S, Kolmar H. Methods Mol Biol. 2018;1685:311-331. doi: 10.1007/978-1-4939-7366-8_19. |
| Generation of potent anti-HER1/2 immunotoxins by protein ligation using split inteins. Pirzer T, Becher KS, Rieker M, Meckel T, Mootz HD, Kolmar H. ACS Chem Biol. 2018 Jun 19. doi: 10.1021/acschembio.8b00222. [Epub ahead of print] PMID: 29920062 |
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Directed Evolution of a Bond-Forming Enzyme: Ultrahigh-Throughput Screening of Microbial Transglutaminase Using Yeast Surface Display. Deweid L, Neureiter L, Englert S, Schneider H, Deweid J, Yanakieva D, Sturm J, Bitsch S, Christmann A, Avrutina O, Fuchsbauer HL, Kolmar H. Chemistry. 2018 Jul 26. doi: 10.1002/chem.201803485. [Epub ahead of print] PMID: 30047596 |
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Engineering Bispecific Antibodies with Defined Chain Pairing. Krah S, Sellmann C, Rhiel L, Schröter C, Dickgießer S, Beck J, Zielonka S, Toleikis L, Hock B, Kolmar H, Becker S. N Biotechnol. 2017 Jan 27. pii: S1871-6784(16)32478-5. doi: 10.1016/j.nbt.2016.12.010. [Epub ahead of print] |
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Generation of human bispecific common light chain antibodies by combining animal immunization and yeast display. Krah S, Schröter C, Eller C, Rhiel L, Rasche N, Beck J, Sellmann C, Günther R, Toleikis L, Hock B, Kolmar H, Becker S. Protein Eng Des Sel. 2017 Jan 5. doi: 10.1093/protein/gzw077. |
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A simplified procedure for antibody engineering by yeast surface display: Coupling display levels and target binding by ribosomal skipping. Grzeschik J, Hinz SC, Könning D, Pirzer T, Becker S, Zielonka S, Kolmar H. Biotechnol J. 2017 Feb;12(2). doi: 10.1002/biot.201600454. |
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Highlight issue: protein design. Sterner R, Höcker B, Kolmar H. Biol Chem. 2017 Jan 1;398(1):1-2. doi: 10.1515/hsz-2016-0322. |
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Camelid and shark single domain antibodies: structural features and therapeutic potential. Könning D, Zielonka S, Grzeschik J, Empting M, Valldorf B, Krah S, Schröter C, Sellmann C, Hock B, Kolmar H. Curr Opin Struct Biol. 2017 Aug;45:10-16. doi: 10.1016/j.sbi.2016.10.019. Epub 2016 Nov 16. Review. |
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Spontaneous Isopeptide Bond Formation as a Powerful Tool for Engineering Site-Specific Antibody-Drug Conjugates. Siegmund V, Piater B, Zakeri B, Eichhorn T, Fischer F, Deutsch C, Becker S, Toleikis L, Hock B, Betz UA, Kolmar H. Sci Rep. 2016 Dec 16;6:39291. doi: 10.1038/srep39291. |
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Semi-synthetic vNAR libraries screened against therapeutic antibodies primarily deliver anti-idiotypic binders. Könning D, Rhiel L, Empting M, Grzeschik J, Sellmann C, Schröter C, Zielonka S, Dickgießer S, Pirzer T, Yanakieva D, Becker S, Kolmar H. Sci Rep. 2017 Aug 29;7(1):9676. doi: 10.1038/s41598-017-10513-9. |
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An Apoptosis-Inducing Peptidic Heptad That Efficiently Clusters Death Receptor 5 Valldorf B, Fittler H, Deweid L, Ebenig A, Dickgiesser S, Sellmann C, Becker J, Zielonka S, Empting M, Avrutina O, Kolmar H. Angew Chem Int Ed Engl. 2016 Mar 15 |
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Spontaneous Isopeptide Bond Formation as a Powerful Tool for Engineering Site-Specific Antibody-Drug Conjugates Siegmund V, Piater B, Zakeri B, Eichhorn T, Fischer F, Deutsch C, Becker S, Toleikis L, Hock B, Betz UA, Kolmar H. Sci Rep. 2016 Dec 16;6:39291. doi: 10.1038/srep39291. |
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Camelid and shark single domain antibodies: structural features and therapeutic potential. Könning D, Zielonka S, Grzeschik J, Empting M, Valldorf B, Krah S, Schröter C, Sellmann C, Hock B, Kolmar H. Curr Opin Struct Biol. 2016 Nov 16;45:10-16. doi: 10.1016/j.sbi.2016.10.019. Review. |
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Nanoscale Biodegradable Organic-Inorganic Hybrids for Efficient Cell Penetration and Drug Delivery. Hörner S, Knauer S, Uth C, Jöst M, Schmidts V, Frauendorf H, Thiele CM, Avrutina O, Kolmar H. Angew Chem Int Ed Engl. 2016 Nov 14;55(47):14842-14846. doi: 10.1002/anie.201606065. |
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Balancing Selectivity and Efficacy of Bispecific Epidermal Growth Factor Receptor (EGFR) × c-MET Antibodies and Antibody-Drug Conjugates. Sellmann C, Doerner A, Knuehl C, Rasche N, Sood V, Krah S, Rhiel L, Messemer A, Wesolowski J, Schuette M, Becker S, Toleikis L, Kolmar H, Hock B. J Biol Chem. 2016 Nov 25;291(48):25106-25119. |
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Structure of the Dispase Autolysis-inducing Protein from Streptomyces mobaraensis and Glutamine Cross-linking Sites for Transglutaminase. Fiebig D, Schmelz S, Zindel S, Ehret V, Beck J, Ebenig A, Ehret M, Fröls S, Pfeifer F, Kolmar H, Fuchsbauer HL, Scrima A. J Biol Chem. 2016 Sep 23;291(39):20417-26. doi: 10.1074/jbc.M116.731109. |
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PROLink-Single Step Circularization and Purification Procedure for the Generation of an Improved Variant of Human Growth Hormone. Rasche N, Tonillo J, Rieker M, Becker S, Dorr B, Ter-Ovanesyan D, Betz UA, Hock B, Kolmar H. Bioconjug Chem. 2016 May 18;27(5):1341-7. doi: 10.1021/acs.bioconjchem.6b00137. |
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Coupled reactions on bioparticles: Stereoselective reduction with cofactor regeneration on PhaC inclusion bodies Spieler V, Valldorf B, Maaß F, Kleinschek A, Hüttenhain SH, Kolmar H. Biotechnol J. 2016 Feb 22 |
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Single-domain antibodies for biomedical applications. Krah S, Schröter C, Zielonka S, Empting M, Valldorf B, Kolmar H. Immunopharmacol Immunotoxicol. 2016;38(1):21-8. doi: 10.3109/08923973.2015.1102934. Review. |
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Isolation of a pH-Sensitive IgNAR Variable Domain from a Yeast-Displayed, Histidine-Doped Master Library Doreen Könning, Stefan Zielonka, Carolin Sellmann, Christian Schröter, Julius Grzeschik, Stefan Becker, Harald Kolmar Mar Biotechnol (NY). 2016 Feb 2 |
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Aptamers Binding to c-Met Inhibiting Tumor Cell Migration Birgit Piater, Achim Doerner, Ralf Guenther, Harald Kolmar, Bjoern Hock PLoS One. 2015 Dec 11 |
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Single-domain antibodies for biomedical applications. Krah S, Schröter C, Zielonka S, Empting M, Valldorf B, Kolmar H. Immunopharmacol Immunotoxicol. 2015 Nov 9:1-8. |
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Engineering a constrained peptidic scaffold towards potent and selective furin inhibitors. Fittler H, Depp A, Avrutina O, Dahms SO, Than ME, Empting M, Kolmar H. Chembiochem. 2015 Oct 1. doi: 10.1002/cbic.201500447. |
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Locked by Design: A Conformationally Constrained Transglutaminase Tag Enables Efficient Site-Specific Conjugation Siegmund V, Schmelz S, Dickgiesser S, Beck J, Ebenig A, Fittler H, Frauendorf H, Piater B, Betz UA, Avrutina O, Scrima A, Fuchsbauer HL, Kolmar H Angew Chem Int Ed Engl. 2015 Sep 14. |
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Self-Assembled Hybrid Aptamer-Fc Conjugates for Targeted Delivery: A Modular Chemoenzymatic Approach Stephan Dickgiesser, Nicolas Rasche, DaichiNasu, Stephen Middel, Sebastian Hörner, Olga Avrutina, Ulf Diederichsen, Harald Kolmar ACS Chem Biol. 2015 Jul 14 |
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Combination of inverse electron-demand Diels-Alder reaction with highly efficient oxime ligation expands the toolbox of site-selective peptide conjugations Sebastian Hörner, Christina Uth, Olga Avrutina, Holm Frauendorf, Manfred Wiessler, Harald Kolmar Chemical Communications, 06/2015; DOI: 10.1039/C5CC03434E |
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The Shark Strikes Twice: Hypervariable Loop 2 of Shark IgNAR Antibody Variable Domains and Its Potential to Function as an Autonomous Paratope Stefan Zielonka, Martin Empting, Doreen Könning, Julius Grzeschik, Simon Krah, Stefan Becker, Stephan Dickgiesser, Harald Kolmar Mar Biotechnol (NY). 2015 May 24 |
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Cystine-knot peptides targeting cancer-relevant human cytotoxic T lymphocyte-associated antigen 4 (CTLA-4) Franziska Maaß, Joycelyn Wüstehube-Lausch, Stephan Dickgießer, Bernhard Valldorf, Michael Reinwarth, Hans-Ulrich Schmoldt, Matin Daneschdar, Olga Avrutina, Ugur Sahin, Harald Kolmar J Pept Sci. 2015 May 10. doi: 10.1002/psc.2782. |
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At-line mid infrared spectroscopy for monitoring downstream processing unit operations Florian Capito, Romas Skudas, Harald Kolmar, PROCESS BIOCHEMISTRY 03/2015 |
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A generic approach to engineer antibody pH-switches using combinatorial histidine scanning libraries and yeast display. Christian Schröter, Ralf Günther, Laura Rhiel, Stefan Becker, Lars Toleikis, Achim Doerner, Janine Becker, Andreas Schönemann, Daichi Nasu, Berend Neuteboom, Harald Kolmar, Björn Hock, MAbs. 2015 Jan 2;7(1):138-51, |
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Structural insights and biomedical potential of IgNAR scaffolds from sharks. Stefan Zielonka, Martin Empting, Julius Grzeschik, Doreen Könning, Caroline J Barelle, Harald Kolmar, MAbs. 2015 Jan 2;7(1):15-25, |
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Bacterial Secretion Systems for Use in Biotechnology: Autotransporter-Based Cell Surface Display and Ultrahigh-Throughput Screening of Large Protein Libraries. Jaeger KE, Kolmar H. Springer Berlin Heidelberg 2015, doi.org/10.1007/8623_2015_125, Buchkapitel |
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REAL-Select: Full-Length Antibody Display and Library Screening by Surface Capture on Yeast Cells Laura Rhiel, Simon Krah, Ralf Günther, Stefan Becker, Harald Kolmar, Björn Hock, PLoS ONE 01/2014; 9(12) |
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Fragmentation follows structure: top-down mass spectrometry elucidates the topology of engineered cystine-knot miniproteins. Reinwarth M, Avrutina O, Fabritz S, Kolmar H. PLoS One. 2014 ;9(10):e108626, |
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Effective PHIP Labeling of Bioactive Peptides Boosts the Intensity of the NMR Signal. Sauer G, Nasu D, Tietze D, Gutmann T, Englert S, Avrutina O, Kolmar H, Buntkowsky G. Angew Chem Int Ed Engl. 2014 ;53(47):12941-5, |
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A Chemoenzymatic Approach to Protein Immobilization onto Crystalline Cellulose Nanoscaffolds. Uth C, Zielonka S, Hörner S, Rasche N, Plog A, Orelma H, Avrutina O, Zhang K, Kolmar H Angew Chem Int Ed Engl. 2014;53(46):12618-23, |
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Shark Attack: High affinity binding proteins derived from shark vNAR domains by stepwise in vitro affinity maturation. Zielonka S, Weber N, Becker S, Doerner A, Christmann A, Christmann C, Uth C, Fritz J, Schäfer E, Steinmann B, Empting M, Ockelmann P, Lierz M, Kolmar H. J Biotechnol. 2014 pii: S0168-1656(14)00204-1, |
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Potent inhibitors of human matriptase-1 based on the scaffold of sunflower trypsin inhibitor. Fittler H, Avrutina O, Empting M, Kolmar H. J Pept Sci. 2014;20(6):415-20, |
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Feasibility of polyelectrolyte-driven Fab fragment separation. Capito F, Kolmar H, Edelmann B, Skudas R. Biotechnol J. 2014;9(5):698-701, |
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A general strategy for antibody library screening via conversion of transient target binding into permanent reporter deposition. Maass A, Heiseler T, Maass F, Fritz J, Hofmeyer T, Glotzbach B, Becker S, Kolmar H, Protein Engineering Design & Selection (2014) 27(2):41-47, |
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Azobenzene switch with a long-lived cis-state to photocontrol the enzyme activity of a histone deacetylase-like amidohydrolase. Korbus M, Balasubramanian G, Muller-Plathe F, Kolmar H, Meyer-Almes FJ, Biological chemistry (2014) 395(4):401-412., |
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Protein production in yarrowia lipolytica via fusion to the secreted lipase lip2p. Hofmeyer T, Bulani SI, Grzeschik J, Krah S, Glotzbach B, Uth C, Avrutina O, Brecht M, Goringer HU, van Zyl P, Kolmar H, Molecular biotechnology (2014) 56(1):79-90. |
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Therapeutic antibody engineering by high efficiency cell screening. Doerner A, Rhiel L, Zielonka S, Kolmar H, FEBS letters (2014) 588(2):278-287. |
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Required polymer lengths per precipitated protein molecule in protein-polymer interaction. Capito F, Kolmar H, Stanislawski B, Skudas R, J Polym Res (2014) 21(2). |
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Feasibility of polyelectrolyte-driven fab fragment separation. Capito F, Kolmar H, Edelmann B, Skudas R, Biotechnology journal (2014) 9(5):698-701. |
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Oxidative folding of peptides with cystine-knot architectures: Kinetic studies and optimization of folding conditions. Reinwarth M, Glotzbach B, Tomaszowski M, Fabritz S, Avrutina O, Kolmar H: Chembiochem : a European journal of chemical biology (2013) 14(1):137-146 |
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Phip-label: Parahydrogen-induced polarization in propargylglycine-containing synthetic oligopeptides. Korner M, Sauer G, Heil A, Nasu D, Empting M, Tietze D, Voigt S, Weidler H, Gutmann T, Avrutina O, Kolmar H et al, Chemical communications (2013) 49(71):7839-7841. |
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Cube-octameric silsesquioxane-mediated cargo peptide delivery into living cancer cells. Hörner S, Fabritz S, Herce HD, Avrutina O, Dietz C, Stark RW, Cardoso MC, Kolmar H, Organic & biomolecular chemistry (2013) 11(14):2258-2265 |
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Arranged sevenfold: Structural insights into the c-terminal oligomerization domain of human c4b-binding protein. Hofmeyer T, Schmelz S, Degiacomi MT, Dal Peraro M, Daneschdar M, Scrima A, van den Heuvel J, Heinz DW, Kolmar H, Journal of molecular biology (2013) 425(8):1302-1317 |
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Structural characterization of spinacia oleracea trypsin inhibitor iii (soti-iii). Glotzbach B, Schmelz S, Reinwarth M, Christmann A, Heinz DW, Kolmar H, Acta Crystallogr D (2013) 69(114-120 |
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Combinatorial optimization of cystine-knot peptides towards high-affinity inhibitors of human matriptase-1. Glotzbach B, Reinwarth M, Weber N, Fabritz S, Tomaszowski M, Fittler H, Christmann A, Avrutina O, Kolmar H, PloS one (2013) 8(10) |
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Performance evaluation of thick film open tubular silica capillary by reversed phase liquid chromatography. Forster S, Kolmar H, Altmaier S, Journal of Chromatography A (2013) 1283(110-115 |
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Preparation and kinetic performance assessment of thick film 10-20 mu m open tubular silica capillaries in normal phase high pressure liquid chromatography. Forster S, Kolmar H, Altmaier S, Journal of Chromatography A (2013) 1315(127-134 |
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Combinatorial tuning of peptidic drug candidates: High-affinity matriptase inhibitors through incremental structure-guided optimization. Fittler H, Avrutina O, Glotzbach B, Empting M, Kolmar H, Organic & biomolecular chemistry (2013) 11(11):1848-1857 |
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Bioconjugation on cube-octameric silsesquioxanes. Fabritz S, Horner S, Avrutina O, Kolmar H, Organic & biomolecular chemistry (2013) 11(14):2224-2236 |
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Matrix effects during monitoring of antibody and host cell proteins using attenuated total reflection spectroscopy. Capito F, Skudas R, Stanislawski B, Kolmar H, Biotechnology progress (2013) 29(1):265-274 |
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Polyelectrolyte-protein interaction at low ionic strength: Required chain flexibility depending on protein average charge. Capito F, Skudas R, Stanislawski B, Kolmar H, Colloid Polym Sci (2013) 291(7):1759-1769 |
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Customization of copolymers to optimize selectivity and yield in polymer-driven antibody purification processes. Capito F, Skudas R, Stanislawski B, Kolmar H, Biotechnology progress (2013) 29(6):1484-1493 |
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Host cell protein quantification by fourier transform mid infrared spectroscopy (ft-mir). Capito F, Skudas R, Kolmar H, Stanislawski B, (2013) 110(1):252-259, Biotechnology and bioengineering |
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Mid-infrared spectroscopy-based antibody aggregate quantification in cell culture fluids. Capito F, Skudas R, Kolmar H, Hunzinger C, Biotechnology journal (2013) 8(8):912-U948 |
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Feasibility study of semi-selective protein precipitation with salt-tolerant copolymers for industrial purification of therapeutic antibodies. Capito F, Bauer J, Rapp A, Schroter C, Kolmar H, Stanislawski B, Biotechnology and bioengineering (2013) 110(11):2915-2927 |
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Autotransporters with gdsl passenger domains: Molecular physiology and biotechnological applications. Wilhelm S, Rosenau F, Kolmar H, Jaeger KE, Chembiochem : a European journal of chemical biology (2011) 12(10):1476-1485 |
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Decorating microbes: Surface display of proteins on escherichia coli. van Bloois E, Winter RT, Kolmar H, Fraaije MW, Trends in biotechnology (2011) 29(2):79-86 |
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DNA libraries for the construction of phage libraries: Statistical and structural requirements and synthetic methods. Lindner T, Kolmar H, Haberkorn U, Mier W, Molecules (2011) 16(2):1625-1641 |
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Natural and engineered cystine knot miniproteins for diagnostic and therapeutic applications. Kolmar H, Current pharmaceutical design (2011) 17(38):4329-4336 |
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„Triazole bridge“: Disulfide-bond replacement by ruthenium-catalyzed formation of 1,5-disubstituted 1,2,3-triazoles. Empting M, Avrutina O, Meusinger R, Fabritz S, Reinwarth M, Biesalski M, Voigt S, Buntkowsky G, Kolmar H, Angew Chem Int Edit (2011) 50(22):5207-5211 |
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Bi-specific aptamers mediating tumor cell lysis. Boltz A, Piater B, Toleikis L, Guenther R, Kolmar H, Hock B, Journal of Biological Chemistry (2011) 286(24):21896-21905 |
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In vivo enzyme immobilization by inclusion body display. Steinmann B, Christmann A, Heiseler T, Fritz J, Kolmar H, Applied and environmental microbiology (2010) 76(16):5563-5569 |
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Engineered cystine knot miniproteins as potent inhibitors of human mast cell tryptase beta. Sommerhoff CP, Avrutina O, Schmoldt HU, Gabrijelcic-Geiger D, Diederichsen U, Kolmar H, Journal of molecular biology (2010) 395(1):167-175 |
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Engineered cystine-knot miniproteins for diagnostic applications. Kolmar H, Expert review of molecular diagnostics (2010) 10(3):361-368 |
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Towards click bioconjugations on cube-octameric silsesquioxane scaffolds. Fabritz S, Heyl D, Bagutski V, Empting M, Rikowski E, Frauendorf H, Balog I, Fessner WD, Schneider JJ, Avrutina O, Kolmar H Organic & biomolecular chemistry (2010) 8(9):2212-2218 |
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Sunflower trypsin inhibitor 1 derivatives as molecular scaffolds for the development of novel peptidic radiopharmaceuticals. Boy RG, Mier W, Nothelfer EM, Altmann A, Eisenhut M, Kolmar H, Tomaszowski M, Kramer S, Haberkorn U, Molecular Imaging and Biology (2010) 12(4):377-385 |
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Biological diversity and therapeutic potential of natural and engineered cystine knot miniproteins. Kolmar H, Curr Opin Pharmacol (2009) 9(5):608-614 |
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Application of copper(i) catalyzed azide-alkyne [3+2] cycloaddition to the synthesis of template-assembled multivalent peptide conjugates. Avrutina O, Empting M, Fabritz S, Daneschdar M, Frauendorf H, Diederichsen U, Kolmar H, Organic & biomolecular chemistry (2009) 7(20):4177-4185 |
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Characterisation of the barrier caused by luminally secreted gastro-intestinal proteolytic enzymes for two novel cystine-knot microproteins. Werle M, Kolmar H, Albrecht R, Bernkop-Schnurch A, Amino Acids (2008) 35(1):195-200 |
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Alternative binding proteins get mature: Rivalling antibodies. Kolmar H, Skerra A, Febs J (2008) 275(11):2667-2667 |
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Alternative binding proteins: Biological activity and therapeutic potential of cystine-knot miniproteins. Kolmar H, Febs J (2008) 275(11):2684-2690 |
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Knottin cyclization: Impact on structure and dynamics. Heitz A, Avrutina O, Le-Nguyen D, Diederichsen U, Hernandez JF, Gracy J, Kolmar H, Chiche L, Bmc Struct Biol (2008) |
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Single-cell high-throughput screening to identify enantioselective hydrolytic enzymes. Becker S, Hobenreich H, Vogel A, Knorr J, Wilhelm S, Rosenau F, Jaeger KE, Reetz MT, Kolmar H, Angew Chem Int Edit (2008) 47(27):5085-5088 |
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Head-to-tail cyclized cystine-knot peptides by a combined recombinant and chemical route of synthesis. Avrutina O, Schmoldt HU, Gabrijelcic-Geiger D, Wentzel A, Frauendorf H, Sommerhoff CP, Diederichsen U, Kolmar H:, Chembiochem : a European journal of chemical biology (2008) 9(1):33-37 |
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Functional cell-surface display of a lipase-specific chaperone. Wilhelm S, Rosenau F, Becker S, Buest S, Hausmann S, Kolmar H, Jaeger KE, Chembiochem : a European journal of chemical biology (2007) 8(1):55-60 |
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Functional genomics of pseudomonas aeruginosa to identify habitat-specific determinants of pathogenicity. Wiehlmann L, Munder A, Adams T, Juhas M, Kolmar H, Salunkhe P, Tummler B, Int J Med Microbiol (2007) 297(7-8):615-623 |
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Relation between scaffold size and membrane bound enzyme caused degradation of two novel cystine knot microproteins. Werle M, Kolmar H, Bernkop-Schnurch A, Lett Drug Des Discov (2007) 4(1):33-36 |
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Evaluation and improvement of the properties of the novel cystine-knot microprotein mcoeeti for oral administration. Werle M, Kafedjiiski K, Kolmar H, Bernkop-Schnurch A, Int J Pharmaceut (2007) 332(1-2):72-79 |
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Grafting of thrombopoietin-mimetic peptides into cystine knot miniproteins yields high-affinity thrombopoietin antagonists and agonists. Krause S, Schmoldt HU, Wentzel A, Ballmaier M, Friedrich K, Kolmar H, Febs J (2007) 274(1):86-95 |
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Crystal structure of the electron transfer complex rubredoxin-rubredoxin reductase of pseudomonas aeruginosa. Hagelueken G, Wiehlmann L, Adams TM, Kolmar H, Heinz DW, Tummler B, Schubert WD, P Natl Acad Sci USA (2007) 104(30):12276-12281 |
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Ultrahigh-throughput screening to identify e-coli cells expressing functionally active enzymes on their surface. Becker S, Michalczyk A, Wilhelm S, Jaeger KE, Kolmar H, Chembiochem : a European journal of chemical biology (2007) 8(8):943-949 |
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The potential of cystine-knot microproteins as novel pharmacophoric scaffolds in oral peptide drug delivery. Werle M, Schmitz T, Huang HL, Wentzel A, Kolmar H, Bernkop-Schnurch A, J Drug Target (2006) 14(3):137-146 |
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Inhibition of platelet aggregation by grafting rgd and kgd sequences on the structural scaffold of small disulfide-rich proteins. Reiss S, Sieber M, Oberle V, Wentzel A, Spangenberg P, Claus R, Kolmar H, Losche W, Platelets (2006) 17(3):153-157 |
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Barnase fusion as a tool to determine the crystal structure of the small disulfide-rich protein mcoeeti. Niemann HH, Schmoldt HU, Wentzel A, Kolmar H, Heinz DW, Journal of molecular biology (2006) 356(1):1-8 |
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The crystal structure of sdsa1, an alkylsulfatase from pseudomonas aeruginosa, defines a third class of sulfatases Hagelueken G, Adams TM, Wiehlmann L, Widow U, Kolmar H, Tummler B, Heinz DW, Schubert WD, (vol 103, pg 7631, 2006). P Natl Acad Sci USA (2006) 103(28):10824-10824 |
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A fusion protein system for the recombinant production of short disulfide bond rich cystine knot peptides using barnase as a purification handle. Schmoldt HU, Wentzel A, Becker S, Kolmar H, Protein Expres Purif (2005) 39(1):82-89 |
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Structure of ecballium elaterium trypsin inhibitor ii (eeti-ii): A rigid molecular scaffold. Kratzner R, Debreczeni JE, Pape T, Schneider TR, Wentzel A, Kolmar H, Sheldrick GM, Uson I, Acta Crystallogr D (2005) 61(1255-1262 |
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A generic system for the escherichia coli cell-surface display of lipolytic enzymes. Becker S, Theile S, Heppeler N, Michalczyk A, Wentzel A, Wilhelm S, Jaeger KE, Kolmar H, FEBS letters (2005) 579(5):1177-1182 |
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Trypsin inhibition by macrocyclic and open-chain variants of the squash inhibitor mcoti-ii. Avrutina O, Schmoldt HU, Gabrijelcic-Geiger D, Le Nguyen D, Sommerhoff CP, Diederichsen U, Kolmar H, Biological chemistry (2005) 386(12):1301-1306 |
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Intimin-mediated export of passenger proteins requires maintenance of a translocation-competent conformation. Adams TM, Wentzel A, Kolmar H, J Bacteriol (2005) 187(2):522-533 |
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Bacteria displaying interleukin-4 mutants stimulate mammalian cells and reflect the biological activities of variant soluble cytokines. Krause S, Wurdemann D, Wentzel A, Christmann A, Fehr H, Kolmar H, Friedrich K: Chembiochem : a European journal of chemical biology (2004) 5(6):804-810 |
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Ultra-high-throughput screening based on cell-surface display and fluorescence-activated cell sorting for the identification of novel biocatalysts. Becker S, Schmoldt HU, Adams TM, Wilhelm S, Kolmar H, Curr Opin Biotech (2004) 15(4):323-329 |
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Fmoc-assisted synthesis of a 29-residue cystine-knot trypsin inhibitor containing a guaninyl amino acid at the p1-position. Avrutina O, Schmoldt HU, Kolmar H, Diederichsen U, Eur J Org Chem (2004) 23):4931-4935 |
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Display of passenger proteins on the surface of escherichia coli k-12 by the enterohemorrhagic e-coli intimin eaea. Wentzel A, Christmann A, Adams T, Kolmar H, J Bacteriol (2001) 183(24):7273-7284 |
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Epitope mapping and affinity purification of monospecific antibodies by escherichia coli cell surface display of gene-derived random peptide libraries. Christmann A, Wentzel A, Meyer C, Meyers G, Kolmar H, J Immunol Methods (2001) 257(1-2):163-173 |
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Expression of two synthetic genes in Escherichia coli and in Staphylococcus carnosus. Friedrich, K., Kolmar, H., Pschorr, J., Wippler, J., Fritz, H.-J. (1990). In: Protein Engineering. Ikehara, M., Oshima, T., Titani, K. (Eds.) Japan Scientific Societies Press, Tokyo, pp. 111-119. |
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Oligonucleotide-directed mutagenesis with single-stranded cloning vectors. Kolmar, H., Fritz, H.-J. (1995). In: DNA Cloning 1: A practical approach. D. Glover, B. D. Hames (Eds.). IRL Press, Oxford, pp. 193-224. |
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Enzyme Engineering by bacterial cell surface display. Adams, T., Kolmar, H. (2002) In: Enzyme functionality: Design, Engineering and Screening. A: Svendson (Ed.). Marcel Dekker, Inc., New York. |
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DegP Protease. Kolmar, H(2004). In: Handbook of Proteolytic Enzymes. 2nd Edition. A.J. Barrett, N. D. Rawlings, F. Woessner (Eds.). Academic Press, New York. |
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FACS Screening of Combinatorial Peptide and Protein Libraries Displayed on the Surface of Escherichia coli Cells. Adams, T., Schmoldt, H.-U., Kolmar, H. (2004) In: Evolutionary Methods in Biotechnology. S: Brakman, A Schwienhorst (Eds.) Wiley-VCH, Weinheim. |
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Microbodies Schmoldt, H.-U., Daneschdar, M., Kolmar, H., Blind, M. (2008) In: Methods in Molecular Biology, Nucleic acid and peptide aptamers”. Humana press. Accepted. |
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Bacterial Secretion Systems for Use in Biotechnology: Autotransporter-Based Cell Surface Display and Ultrahigh-Throughput Screening of Large Protein Libraries. Karl-erich Jaeger and Harald Kolmar In:Hydrocarbon and Lipid Microbiology Protocols. Springer. |
A TRANSGLUTAMINE TAG FOR EFFICIENT SITE-SPECIFIC BIOCONJUGATION
Publication number: 20190194344
Abstract: The present invention provides novel peptide sequences for use in microbial transgluatminase-mediated, in particular mTG2-mediated bioconjugations, in particular for the manufacture of antibody-drug-conjugates. Further disclosed are bioconjugation methods employing mTG2 and the novel peptide sequence motifs of the invention. The present invention further provides proteins comprising the novel sequence motifs of the invention as well as polynucleotides encoding the same.
Type: Application
Filed: August 4, 2016
Publication date: June 27, 2019
Applicant: Merck Patent GmbH
Inventors: Birgit Piater, Ulrich Betz, Harald Kolmar, Vanessa Siegmund
METHODS FOR GENERATING BISPECIFIC SHARK VARIABLE ANTIBODY DOMAINS AND USE THEREOF
Publication number: 20180171020
Abstract: The present invention provides a method for generating bispecific shark variable antibody domains (vNAR domains) and uses thereof. The present invention further provides fusion proteins comprising the inventive bispecific vNAR domains as well as polynucleotide libraries for use in the generation of the inventive bi-specific vNARs. Furthermore, the invention provides pharmaceutical compositions comprising the inventive bispecific vNARs or fusion proteins comprising bi-specific vNAR domains for use in the treatment of pathological conditions in an individual. The invention also provides kits of parts comprising the bispecific vNAR domains or fusion proteins.
Type: Application
Filed: October 21, 2015
Publication date: June 21, 2018
Applicant: Merck Patent GmbH
Inventors: Stefan Becker, Bjoern Hock, Stefan Zielonka, Harald Kolmar, Martin Empting
General strategy for antibody library screening
Patent number: 9733240
Abstract: A generally applicable method for the selective covalent attachment of a reporter molecule to a replicating entity that allows one to obtain specific binders from a single round of library screening is disclosed. For example, selective biotinylation of phage particles and yeast cells displaying a binder to any given target can be achieved via application of a coupled enzyme reaction that includes a peroxidase, an oxidase and a catalase.
Type: Grant
Filed: December 14, 2012
Date of Patent: August 15, 2017
Assignee: Merck Patents GmbH
Inventors: Stefan Becker, Tim Heiseler, Alexander Maass, Harald Kolmar
METHOD FOR PEPTIDE SYNTHESIS AND APPARATUS FOR CARRYING OUT A METHOD FOR SOLID PHASE SYNTHESIS OF PEPTIDES
Publication number: 20170218010
Abstract: The invention relates to a method for peptide synthesis, wherein said method comprises the steps of reacting a first amino acid or a first peptide with an ?-amine protected second amino acid in a solvent selected from the group consisting of water, alcohol, and a mixture of water and alcohol, and removing the ?-amine protecting group with a deprotecting solution. The invention further relates to protective agents, their use and an apparatus for carrying out a method for solid phase synthesis of peptides.
Type: Application
Filed: September 29, 2015
Publication date: August 3, 2017
Inventors: Sascha KNAUER, Tobias Michael Louis ROESE, Olga AVRUTINA, Harald KOLMAR, Christina UTH
POTENT INHIBITORS OF HUMAN MATRIPTASE DERIVED FROM MCOTI-II VARIANTS
Publication number: 20160194380
Abstract: The present invention pertains to highly potent Matriptase inhibitors derived from the miniprotein McotI-II.
Type: Application
Filed: April 8, 2014
Publication date: July 7, 2016
Applicant: Merck Patent GmbH
Inventors: Michael TOMASZOWSKY, Niklas WEBER, Bernhard GLOTZBACH, Harald KOLMAR, Bjoern HOCK
HIGH-AFFINITY MATRIPTASE INHIBITORS
Publication number: 20160016998
Abstract: The present invention relates to novel matriptase inhibitors.
Type: Application
Filed: January 9, 2014
Publication date: January 21, 2016
Applicant: Merck Patent GmbH
Inventor: Harald KOLMAR
GENERAL STRATEGY FOR ANTIBODY LIBRARY SCREENING
Publication number: 20140357514
Abstract: A generally applicable method for the selective covalent attachment of a reporter molecule to a replicating entity that allows one to obtain specific binders from a single round of library screening is disclosed. For example, selective biotinylation of phage particles and yeast cells displaying a binder to any given target can be achieved via application of a coupled enzyme reaction that includes a peroxidase, an oxidase and a catalase.
Type: Application
Filed: December 14, 2012
Publication date: December 4, 2014
Inventors: Stefan Becker, Tim Heiseler, Alexander Maass, Harald Kolmar
Use of microproteins as tryptase inhibitors
Patent number: 8278262
Abstract: Disclosed are uses of microproteins preferably microproteins forming a cystine knot (i.e. belonging to the family of inhibitor cystine knot (ICK) polypeptides) or polynucleotides encoding said microproteins for the preparation of a pharmaceutical composition for treating or preventing a disease that can be treated or prevented by inhibiting the activity of tryptase as well as corresponding methods of treatment. Also disclosed are uses of the microproteins for inhibiting tryptase activity, for purifying tryptase, as a carrier molecule for tryptase and for deleting or quantifying tryptase in a sample, including corresponding diagnostic applications. Furthermore disclosed are fusion proteins comprising an inactive barnase as well as fusion proteins comprising barnase and a microprotein. Also encompassed are nucleic acid molecules encoding such a fusion protein, as well as corresponding vectors, host cells, preparation methods and uses of the fusion protein.
Type: Grant
Filed: September 19, 2005
Date of Patent: October 2, 2012
Assignee: BioNTech AG
Inventors: Harald Kolmar, Christian Sommerhoff, Alexander Wentzel
Dimeric or multimeric microproteins
Patent number: 8258258
Abstract: Disclosed is a polypeptide comprising at least two microproteins, which preferably comprise an amino acid sequence having a specific binding activity to a target protein. Furthermore, disclosed are polynucleotides encoding such a polypeptide as well as pharmaceutical compositions and kits comprising said polypeptide or polynucleotide. Also disclosed herein are methods of treatments and second medical uses applying the disclosed polypeptide or polynucleotide. Additionally, the disclosure of the present application relates to a method for forming a covalent bond in a microprotein which can be used for producing the disclosed polypeptides.
Type: Grant
Filed: March 9, 2006
Date of Patent: September 4, 2012
Assignee: BioNTech AG
Inventors: Harald Kolmar, Ernst Boehnlein, Alexander Wentzel, Hans-Ulrich Schmoldt
Polypeptide comprising a knottin protein moiety
Publication number: 20100267610
Abstract: A polypeptide, with an amino acid sequence different from that of knottin protein, having a scaffold moiety with a helix moiety inserted in the scaffold moiety is described. The scaffold moiety comprises a knottin protein, or a fragment of knottin protein.
Type: Application
Filed: February 18, 2008
Publication date: October 21, 2010
Applicant: BIONTECH AG
Inventors: Michael Blind, Harald Kolmar
Dimeric or Multimeric Microproteins
Publication number: 20090156476
Abstract: Disclosed is a polypeptide comprising at least two microproteins, which preferably comprise an amino acid sequence having a specific binding activity to a target protein. Furthermore, disclosed are polynucleotides encoding such a polypeptide as well as pharmaceutical compositions and kits comprising said polypeptide or polynucleotide. Also disclosed herein are methods of treatments and second medical uses applying the disclosed polypeptide or polynucleotide. Additionally, the disclosure of the present application relates to a method for forming a covalent bond in a microprotein which can be used for producing the disclosed polypeptides.
Type: Application
Filed: March 9, 2006
Publication date: June 18, 2009
Applicant: NascaCell Technologies AG
Inventors: Harald Kolmar, Ernst Boehnlein, Alexander Wentzel, Hans-Ulrich Schmoldt
Use of microproteins as tryptase
Publication number: 20090130692
Abstract: Disclosed are uses of microproteins preferably microproteins forming a cystine knot (i.e. belonging to the family of inhibitor cystine knot (ICK) polypeptides) or polynucleotides encoding said microproteins for the preparation of a pharmaceutical composition for treating or preventing a disease that can be treated or prevented by inhibiting the activity of tryptase as well as corresponding methods of treatment. Also disclosed are uses of the microproteins for inhibiting tryptase activity, for purifying tryptase, as a carrier molecule for tryptase and for deleting or quantifying tryptase in a sample, including corresponding diagnostic applications. Furthermore disclosed are fusion proteins comprising an inactive barnase as well as fusion proteins comprising barnase and a microprotein. Also encompassed are nucleic acid molecules encoding such a fusion protein, as well as corresponding vectors, host cells, preparation methods and uses of the fusion protein.
Type: Application
Filed: September 19, 2005
Publication date: May 21, 2009
Applicant: Nasca Cell Technologies AG
Inventors: Harald Kolmar, Christian Sommerhoff, Alexander Wentzel
Method for exposing peptides and polypeptides on the cell surface of bacteria
Patent number: 7186524
Abstract: The inventive method allows peptides or polypeptides to be exposed on the surface of gram-negative host bacteria using specific intimin-based anchor modules. Intimins with shortened carboxy terminals have been found to be particularly suitable anchor modules for passenger domains in the exterior E. coli cell membrane. According to the method, host bacteria are transformed using vectors, on which are located a fused nucleic acid sequence consisting of a sequence segment which codes for an intimin with a shortened carboxy terminal and a nucleic acid sequence segment which codes for the passenger peptide that is to be exposed. The invention permits a particularly large number of passenger domains to be exposed on the cell surface of the bacteria, without adversely affecting the viability of the bacteria.
Type: Grant
Filed: October 25, 2001
Date of Patent: March 6, 2007
Assignee: NascaCell Technologies AG
Inventors: Harald Kolmar, Andreas Christmann, Alexander Wentzel
Method for exposing peptides and polypeptides on the cell surface of bacteria
Publication number: 20040106118
Abstract: The inventive method allows peptides or polypeptides to be exposed on the surface of gram-negative host bacteria using specific intimin-based anchor modules. Intimins with shortened carboxy terminals have been found to be particularly suitable anchor modules for passenger domains in the exterior E.coli cell membrane. According to said method, host bacteria are transformed using vectors, on which are located a fused nucleic acid sequence consisting of a sequence segment which codes for an intimin with a shortened carboxy terminal and a nucleic acid sequence segment which codes for the passenger peptide that is to be exposed. The invention permits a particularly large number of passenger domains to be exposed on the cell surface of the bacteria, without adversely affecting the viability of the bacteria.
Type: Application
Filed: October 15, 2003
Publication date: June 3, 2004
Inventors: Harald Kolmar, Andreas Christmann, Alexander Wentzel
Vectors for the genetic selection of ligand binding proteins in microorganisms by means of signal transduction
Patent number: 5882924
Abstract: The invention relates to a process for the genetic selection in microorganisms of proteins which are capable of ligand binding, in which process a protein which is capable of ligand binding is presented extracytoplasmically and the signal of the ligand binding is passed on by signal transduction to the biosynthetic machinery of the micoorganism for the purpose of expressing a detectable and/or selectable function. In addition to this, the patent discloses microorganisms which are suitable for use in this process, as well as replicons and processes for their preparation.
Type: Grant
Filed: October 22, 1997
Date of Patent: March 16, 1999
Assignee: Behringwerke Aktiengesellschaft
Inventors: Hans-Joachim Fritz, Frank Hennecke, Harald Kolmar
