Entanglement Model of Antibody Viscosity
| Autor: | Christopher E. Woods, Shradha Mishra, Randal R. Ketchem, Feng He, Bruce A. Kerwin, Jeremy D. Schmit |
|---|---|
| Rok vydání: | 2014 |
| Předmět: |
Globular protein
Antigen-Antibody Complex Quantum entanglement Power law Protein Aggregates Viscosity Elastic Modulus Materials Chemistry Molecule Statistical physics Physical and Theoretical Chemistry chemistry.chemical_classification Chemistry Antibodies Monoclonal Polymer Surfaces Coatings and Films Solutions Kinetics Reptation Models Chemical Chemical physics Immunoglobulin G Volume fraction Thermodynamics Streptavidin Protein Binding |
| Zdroj: | The Journal of Physical Chemistry B. 118:5044-5049 |
| ISSN: | 1520-5207 1520-6106 |
| Popis: | Antibody solutions are typically much more viscous than solutions of globular proteins at equivalent volume fraction. Here we propose that this is due to molecular entanglements that are caused by the elongated shape and intrinsic flexibility of antibody molecules. We present a simple theory in which the antibodies are modeled as linear polymers that can grow via reversible bonds between the antigen binding domains. This mechanism explains the observation that relatively subtle changes to the interparticle interaction can lead to large changes in the viscosity. The theory explains the presence of distinct power law regimes in the concentration dependence of the viscosity as well as the correlation between the viscosity and the charge on the variable domain in our antistreptavidin IgG1 model system. |
| Databáze: | OpenAIRE |
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