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Trends Biotechnol. 2014 Jul;32(7):372-80. doi: 10.1016/j.tibtech.2014.05.005. Epub 2014 Jun 4.

Therapeutic protein aggregation: mechanisms, design, and control.

Author information

  • 1Department of Chemical and Biomolecular Engineering, University of Delaware, Newark, DE 19716, USA. Electronic address: cjr@udel.edu.

Abstract

Although it is well known that proteins are only marginally stable in their folded states, it is often less well appreciated that most proteins are inherently aggregation-prone in their unfolded or partially unfolded states, and the resulting aggregates can be extremely stable and long-lived. For therapeutic proteins, aggregates are a significant risk factor for deleterious immune responses in patients, and can form via a variety of mechanisms. Controlling aggregation using a mechanistic approach may allow improved design of therapeutic protein stability, as a complement to existing design strategies that target desired protein structures and function. Recent results highlight the importance of balancing protein environment with the inherent aggregation propensities of polypeptide chains.

Copyright © 2014 Elsevier Ltd. All rights reserved.

KEYWORDS:

computational design; protein aggregation; protein interactions; protein stability

PMID:
24908382
[PubMed - indexed for MEDLINE]
PMCID:
PMC4146573
Free PMC Article
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