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Aggregation of therapeutic proteins.


Aggregation of therapeutic proteins.

Ed. by Wei Wang and Christopher J. Roberts.

John Wiley & Sons


486 pages




Perhaps the most common and most troubling manifestation of protein instability during the development of protein biotherapeutics is the tendency for them to glom together, after which they do not work very well if at all. Researchers at drug companies and university laboratories explore the problem, its causes, its effects, and measures to prevent it. Among their topics are fundamental structures and behaviors of proteins; protein aggregation pathways, kinetics, and thermodynamics; the identification and impact of aggregate-prone regions in proteins and therapeutic monoclonal antibodies; external factors affecting protein aggregation; experimental detection and characterization of protein aggregates; approaches to controlling it during bulk production; effects of formulation interfaces, and drug product manufacturing operations on aggregation and particle formation; approaches to managing it in product development; aggregation and immunogenicity of therapeutic proteins; and a regulatory perspective on aggregates as a product quality attribute.

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Publication:SciTech Book News
Article Type:Book review
Date:Dec 1, 2010
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