Issue 48, 2019
From the journal:

Chemical Science

Synthesis of montbretin A analogues yields potent competitive inhibitors of human pancreatic α-amylase†

Christina R. Tysoe,a   Sami Caner,b   Matthew B. Calvert,a   Anna Win-Mason,a   Gary D. Brayerb  and  Stephen G. Withers ORCID logo *a  

* Corresponding authors

a Department of Chemistry, University of British Columbia, 2036 Main Mall, Vancouver BC, Canada V6T 1Z1
E-mail: withers@chem.ubc.ca

b Department of Biochemistry and Molecular Biology, University of British Columbia, 2350 Health Sciences Mall, Vancouver BC, Canada V6T 1Z3

Abstract

Simplified analogues of the potent human amylase inhibitor montbretin A were synthesised and shown to bind tightly, KI = 60 and 70 nM, with improved specificity over medically relevant glycosidases, making them promising candidates for controlling blood glucose. Crystallographic analysis confirmed similar binding modes and identified new active site interactions.

Graphical abstract: Synthesis of montbretin A analogues yields potent competitive inhibitors of human pancreatic α-amylase

About
Cited by
Related
Download options Please wait...

Supplementary files

Article information

DOI
https://doi.org/10.1039/C9SC02610J
Article type
Edge Article
Submitted
29 May 2019
Accepted
16 Oct 2019
First published
18 Oct 2019
This article is Open Access

All publication charges for this article have been paid for by the Royal Society of Chemistry
Creative Commons BY-NC license

Chem. Sci., 2019,10, 11073-11077

Permissions

Request permissions

Synthesis of montbretin A analogues yields potent competitive inhibitors of human pancreatic α-amylase

C. R. Tysoe, S. Caner, M. B. Calvert, A. Win-Mason, G. D. Brayer and S. G. Withers, Chem. Sci., 2019, 10, 11073 DOI: 10.1039/C9SC02610J

This article is licensed under a Creative Commons Attribution-NonCommercial 3.0 Unported Licence. You can use material from this article in other publications, without requesting further permission from the RSC, provided that the correct acknowledgement is given and it is not used for commercial purposes.

To request permission to reproduce material from this article in a commercial publication, 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 commercial 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