Both reversible self-association and structural changes underpin molecular viscoelasticity of mAb solutions

Both reversible self-association and structural changes underpin molecular viscoelasticity of mAb solutions

The role of antibody structure (conformation) in solution rheology is probed. It is demonstrated here that pH-dependent changes in the tertiary structure of 2 mAb solutions lead to viscoelasticity and not merely a shear viscosity (η) increase. Steady shear flow curves on mAb solutions are reported o...

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Bibliographic Details
Main Authors: Sarangapani, Prasad S., Weaver, Justin, Parupudi, Arun, Besong, Tabot M.D., Adams, Gary G., Harding, Stephen E., Manikwar, Prakash, Castellanos, Maria M., Bishop, Steven M., Pathak, Jai A.
Format: Article
Published: Elsevier 2016
Subjects:
viscosity; protein structure; mAb; light scattering (dynamic); calorimetry (DSC); rheology; analytical ultra-centrifugation; diffusion; protein formulation; protein aggregation
Online Access:https://eprints.nottingham.ac.uk/42598/

Internet

https://eprints.nottingham.ac.uk/42598/

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