期刊
TRENDS IN BIOTECHNOLOGY
卷 32, 期 7, 页码 372-380出版社
ELSEVIER SCIENCE LONDON
DOI: 10.1016/j.tibtech.2014.05.005
关键词
protein aggregation; protein stability; protein interactions; computational design
资金
- National Science Foundation
- National Institutes of Health
- Directorate For Engineering
- Div Of Chem, Bioeng, Env, & Transp Sys [1264329] Funding Source: National Science Foundation
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.
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