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Issue 23, 2017
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Scandium(III) triflate-promoted serine/threonine-selective peptide bond cleavage

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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

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Publication details

The article was received on 29 Dec 2016, accepted on 23 Jan 2017 and first published on 23 Jan 2017


Article type: Communication
DOI: 10.1039/C6CC10300F
Citation: Chem. Commun., 2017,53, 3311-3314

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    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

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