Scandium(iii) triflate-promoted serine/threonine-selective peptide bond cleavage.

Author(s) Ni, J.; Sohma, Y.; Kanai, M.
Journal Chem Commun (Camb)
Date Published 2017 Mar 16
Abstract

The site-selective cleavage of peptide bonds is an important chemical modification that is useful not only for the structural determination of peptides, but also as an artificial modulator of peptide/protein function and properties. Here we report site-selective hydrolysis of peptide bonds at the Ser and Thr positions with a high conversion yield. This chemical cleavage relies on Sc(iii)-promoted N,O-acyl rearrangement and subsequent hydrolysis. The method is applicable to a broad scope of polypeptides with various functional groups, including a post-translationally modified peptide that is unsuitable for enzymatic hydrolysis. The system was further extended to site-selective cleavage of a native protein, Aβ1-42, which is closely related to the onset of Alzheimer's disease.

DOI 10.1039/c6cc10300f
ISSN 1364-548X
Citation Ni J, Sohma Y, Kanai M. Scandium(iii) triflate-promoted serine/threonine-selective peptide bond cleavage. Chem Commun (Camb). 2017;53(23):3311-3314.

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