Therapeutic protein aggregation: mechanisms, design, and control.
Therapeutic protein aggregation: mechanisms, design, and control.
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DOI：
10.1016/j.tibtech.2014.05.005
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发表时间：
2014-07
影响因子：
17.3
通讯作者：
Roberts, Christopher J.
中科院分区：
文献类型：
--
作者：
Roberts, Christopher J.
虽然众所周知，蛋白质在折叠状态下只是略微稳定，但人们往往不太了解大多数蛋白质在未折叠或部分未折叠状态下天生容易聚集，由此产生的聚集可以非常稳定和持久。对于治疗性蛋白质，聚集体是患者有害免疫反应的重要风险因素，并可通过多种机制形成。使用机械方法控制聚集可能允许改进治疗性蛋白质稳定性的设计，作为针对所需蛋白质结构和功能的现有设计策略的补充。最近的结果强调了平衡蛋白质环境和多肽链固有聚集倾向的重要性。
While 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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影响因子：
3.8
作者：
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发表时间：
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影响因子：
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通过吸附到不锈钢引起的单克隆抗体的聚集。
影响因子：
3.8
作者：
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通讯作者：
Randolph, Theodore W.