Promoting peptide α-helix formation with dynamic covalent oxime side-chain cross-links
Promoting peptide α-helix formation with dynamic covalent oxime side-chain cross-links
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DOI：
10.1039/c1cc12010g
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发表时间：
2011-01-01
影响因子：
4.9
通讯作者：
Horne, W. Seth
中科院分区：
文献类型：
--
作者：
Haney, Conor M.;Loch, Matthew T.;Horne, W. Seth
共价侧链交联已被证明是控制肽折叠的可行策略。我们在此报道，肟侧链键可以在水溶液中从肽中引发α螺旋折叠。生物正交桥在中性缓冲条件下快速形成，所得环状肟能够进行动态共价交换。
Covalent side-chain cross-linking has been shown to be a viable strategy to control peptide folding. We report here that an oxime side-chain linkage can elicit alpha-helical folds from peptides in aqueous solution. The bio-orthogonal bridge is formed rapidly under neutral buffered conditions, and the resulting cyclic oximes are capable of dynamic covalent exchange.