Replacement of the CysA7–CysB7 disulfide bond with a 1,2,3-triazole linker causes unfolding in insulin glargine-Reference-Cited by-同舟云学术

Replacement of the CysA7–CysB7 disulfide bond with a 1,2,3-triazole linker causes unfolding in insulin glargine

Published:2015 Issue:13 Volume:13 Page:4059-4063
ISSN:1477-0520
Container-title:Organic & Biomolecular Chemistry
language:en
Short-container-title:Org. Biomol. Chem.

Author:

Williams Geoffrey M.¹²³⁴,Lee Kathryn⁵²³⁴,Li Xun⁵²³⁴,Cooper Garth J. S.⁵²³⁴,Brimble Margaret A.¹²³⁴⁶

Affiliation:

1. The School of Chemical Sciences

2. University of Auckland

3. Auckland 1010

4. New Zealand

5. The School of Biological Sciences

6. Maurice Wilkins Centre for Molecular Biodiscovery

Abstract

Two analogues of insulin glargine containing a 1,4-disubstituted 1,2,3-triazole group in place of the CysA7–CysB7 disulfide bond were prepared using CuAAC click chemistry to efficiently join the peptide chains.

Publisher

Royal Society of Chemistry (RSC)

Subject

Organic Chemistry,Physical and Theoretical Chemistry,Biochemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2015/OB/C5OB00160A

Reference29 articles.

1. The twentieth century struggle to decipher insulin signalling

2. The disulphide bonds of insulin

3. The Synthesis of Bovine Insulin by the Solid Phase Method1

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