Noncovalent Modification of Chymotrypsin Surface Using an Amphiphilic Polymer Scaffold: Implications in Modulating Protein Function

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• 作者：Britto S. Sandanaraj ; Dharma Rao Vutukuri ; Joseph M. Simard ; Akamol Klaikherd ; Rui Hong ; Vincent M. Rotello ; and S. Thayumanavan
• 刊名：Journal of the American Chemical Society
• 出版年：2005
• 出版时间：August 3, 2005
• 年：2005
• 卷：127
• 期：30
• 页码：10693 - 10698
• 全文大小：244K
• 年卷期：v.127,no.30(August 3, 2005)
• ISSN：1520-5126

文摘

We report here on a new amphiphilic homopolymer that binds noncovalently to proteins. Thispolymer not only binds to the target protein chymotrypsin with submicromolar affinity but also stabilizes thenative structure of the protein. Since the polymer-protein binding process is based on electrostaticinteraction, the bound protein can be released from the polymer surface and reactivated either by increasingthe ionic strength or by adding complementary cationic surfactants. The electrostatic binding of polymer tothe protein results in a marked change in the substrate specificity of chymotrypsin.