No ordinary proteins: Adsorption and molecular orientation of monoclonal antibodies

Author:

Kanthe Ankit1ORCID,Ilott Andrew2,Krause Mary2ORCID,Zheng Songyan2,Li Jinjiang3ORCID,Bu Wei4ORCID,Bera Mrinal K.4ORCID,Lin Binhua4ORCID,Maldarelli Charles15ORCID,Tu Raymond S.1ORCID

Affiliation:

1. Department of Chemical Engineering, The City College of New York, New York, NY 10031, USA.

2. Drug Product Development, Bristol Myers Squibb, New Brunswick, NJ 08901, USA.

3. Pharmaceutical Development, Wolfe Laboratories, Watertown, MA, 01801, USA.

4. NSF’s ChemMatCARS, Center for Advanced Radiation Sources, University of Chicago, Chicago, IL 606371, USA.

5. Levich Institute, The City College of New York, New York, NY 10031, USA.

Abstract

Antibodies adsorbing to the interface are shown to dynamically reorient and unfold to define a quasi-equilibrium state.

Funder

National Science Foundation

Bristol-Myers Squibb

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

Reference58 articles.

1. D. Möbius R. Miller Proteins at Liquid Interfaces (Elsevier 1998).

2. Kinetics of protein unfolding at interfaces

3. Interfacial rheological properties of adsorbed protein layers and surfactants: a review

4. Shear and Dilatational Relaxation Mechanisms of Globular and Flexible Proteins at the Hexadecane/Water Interface

5. E. Dickinson R. Miller Food Colloids: Fundamentals of Formulation vol. 258 (Royal Society of Chemistry 2001).

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