期刊
CHEMICAL COMMUNICATIONS
卷 47, 期 39, 页码 10915-10917出版社
ROYAL SOC CHEMISTRY
DOI: 10.1039/c1cc12010g
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资金
- University of Pittsburgh
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.
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