Relationship between side-chain branching and stoichiometry in 尾³-peptide bundles

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• 作者：Pam Shou-Ping Wang^a ; Cody J. Craig^a ; Alanna Schepartz^a ; ^b ; ^{alanna.schepartz@yale.edu}
• 关键词：Biomaterial ; Protein design ; Protein folding ; Self-assembly
• 刊名：Tetrahedron
• 出版年：2012
• 期刊代码：107_00404020
• 类别：ch
• 出版时间：10 June, 2012
• 卷：68
• 期：23
• 页码：4342-4345
• 文件大小：562 K

摘要

The stability and stoichiometry of 尾³-peptide bundles is influenced by side-chain identity. Previously reported 尾³-peptides containing 尾³-homoleucine on one helical face assemble into octamers, whereas those containing 尾³-homovaline form tetramers. The side chains of 尾³-homoleucine and 尾³-homovaline differ in terms of both side-chain length and 纬-carbon branching. To evaluate the extent to which these two parameters control 尾³-peptide bundle stoichiometry, we synthesized the 尾³-peptide Acid-3Y, which contains 尾³-homoisoleucine in place of 尾³-homoleucine or 尾³-homovaline on one helical face. Acid-3Y assembles into a stable tetramer whose stability resembles that of the previously characterized Acid-VY tetramer. These results suggest that 尾³-peptide bundle stoichiometry can be modulated by the presence or absence of 纬-carbon branching on core side chains.