Promoting peptide α-helix formation with dynamic covalent oxime side-chain cross-links.
نویسندگان
چکیده
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 α-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.
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ورودعنوان ژورنال:
- Chemical communications
دوره 47 39 شماره
صفحات -
تاریخ انتشار 2011