Behavior of Water Near Multimodal Chromatography Ligands and Its Consequences for Modulating Protein–Ligand Interactions-Reference-Cited by-同舟云学术

Behavior of Water Near Multimodal Chromatography Ligands and Its Consequences for Modulating Protein–Ligand Interactions

Published:2021-06-07 Issue:23 Volume:125 Page:6112-6120
ISSN:1520-6106
Container-title:The Journal of Physical Chemistry B
language:en
Short-container-title:J. Phys. Chem. B

Author:

Bilodeau Camille L.¹²^ORCID,Lau Edmond Y.³,Roush David J.⁴,Snyder Mark A.⁵,Cramer Steven M.¹^ORCID

Affiliation:

1. Howard P. Isermann Department of Chemical and Biological Engineering and Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, 110 Eighth Street, Troy, New York 12180, United States

2. Department of Chemical Engineering, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, United States

3. Physical and Life Sciences Directorate, Lawrence Livermore National Laboratory, Livermore, California 94550, United States

4. Biologics Process R&D, Merck & Co., Inc., 2000 Galloping Hill Road, Kenilworth, New Jersey 07033, United States

5. Process Chromatography Division, Bio-Rad Laboratories, 6000 James Watson Drive, Hercules, California 94547, United States

Funder

Department of Energy, Labor and Economic Growth

National Science Foundation

Publisher

American Chemical Society (ACS)

Subject

Materials Chemistry,Surfaces, Coatings and Films,Physical and Theoretical Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.jpcb.1c01549

Reference61 articles.

1. Multimodal Chromatography for Purification of Biotherapeutics – A Review

2. Downstream bioprocessing: recent advances and future promise

3. Investigation of protein selectivity in multimodal chromatography usingin silicodesigned Fab fragment variants

4. Probing multimodal ligand binding regions on ubiquitin using nuclear magnetic resonance, chromatography, and molecular dynamics simulations

5. Mechanistic modeling based process development for monoclonal antibody monomer-aggregate separations in multimodal cation exchange chromatography

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