Department of Chemistry, University of Pittsburgh, Pittsburgh, PA 15260, USA.
Chem Commun (Camb). 2011 Oct 21;47(39):10915-7. doi: 10.1039/c1cc12010g. Epub 2011 Jun 20.
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.
共价侧链交联已被证明是控制肽折叠的一种可行策略。我们在这里报告，肟侧链键可以在水溶液中诱导肽形成α-螺旋折叠。在中性缓冲条件下，生物正交桥快速形成，所得的环状肟能够进行动态共价交换。
