Exploring preferred binding domains of IgG1 mAbs to multimodal adsorbents using a combined biophysics and simulation approach.
Autor: | Dhingra K; Howard P. Isermann Department of Chemical and Biological Engineering, Rensselaer Polytechnic Institute, Troy, New York, USA.; Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, New York, USA., Sinha I; Howard P. Isermann Department of Chemical and Biological Engineering, Rensselaer Polytechnic Institute, Troy, New York, USA.; Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, New York, USA., Snyder M; Process Chemistry Division, Bio-Rad Laboratories, Hercules, California, USA., Roush D; Process R&D, Merck &Co., Inc., Rahway, New Jersey, USA., Cramer SM; Howard P. Isermann Department of Chemical and Biological Engineering, Rensselaer Polytechnic Institute, Troy, New York, USA.; Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, New York, USA. |
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Jazyk: | angličtina |
Zdroj: | Biotechnology progress [Biotechnol Prog] 2024 Mar-Apr; Vol. 40 (2), pp. e3415. Date of Electronic Publication: 2023 Dec 03. |
DOI: | 10.1002/btpr.3415 |
Abstrakt: | In this work, we employ a recently developed biophysical technique that uses diethylpyrocarbonate (DEPC) covalent labeling and mass spectrometry for the identification of mAb binding patches to two multimodal cation exchange resins at different pH. This approach compares the labeling results obtained in the bound and unbound states to identify residues that are sterically shielded and thus located in the mAb binding domains. The results at pH 6 for one mAb (mAb B) indicated that while the complementarity determining region (CDR) had minimal interactions with both resins, the F (© 2023 American Institute of Chemical Engineers.) |
Databáze: | MEDLINE |
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