Issue 23, 2017

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

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.

Graphical abstract: Scandium(iii) triflate-promoted serine/threonine-selective peptide bond cleavage

Supplementary files

Article information

Article type
Communication
Submitted
29 Dec 2016
Accepted
23 Jan 2017
First published
23 Jan 2017

Chem. Commun., 2017,53, 3311-3314

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

J. Ni, Y. Sohma and M. Kanai, Chem. Commun., 2017, 53, 3311 DOI: 10.1039/C6CC10300F

To request permission to reproduce material from this article, please go to the Copyright Clearance Center request page.

If you are an author contributing to an RSC publication, you do not need to request permission provided correct acknowledgement is given.

If you are the author of this article, you do not need to request permission to reproduce figures and diagrams provided correct acknowledgement is given. If you want to reproduce the whole article in a third-party publication (excluding your thesis/dissertation for which permission is not required) please go to the Copyright Clearance Center request page.

Read more about how to correctly acknowledge RSC content.

Social activity

Spotlight

Advertisements