溶解度
合理设计
生化工程
蛋白质工程
突变体
计算生物学
组合化学
化学
肽
计算机科学
生物化学
纳米技术
生物
材料科学
有机化学
工程类
酶
基因
作者
Pietro Sormanni,Francesco A. Aprile,Michele Vendruscolo
标识
DOI:10.1016/j.jmb.2014.09.026
摘要
Protein solubility is often an essential requirement in biotechnological and biomedical applications. Great advances in understanding the principles that determine this specific property of proteins have been made during the past decade, in particular concerning the physicochemical characteristics of their constituent amino acids. By exploiting these advances, we present the CamSol method for the rational design of protein variants with enhanced solubility. The method works by performing a rapid computational screening of tens of thousand of mutations to identify those with the greatest impact on the solubility of the target protein while maintaining its native state and biological activity. The application to a single-domain antibody that targets the Alzheimer's Aβ peptide demonstrates that the method predicts with great accuracy solubility changes upon mutation, thus offering a cost-effective strategy to help the production of soluble proteins for academic and industrial purposes.
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