Issue 1, 2019

Crystallographic and SAR analyses reveal the high requirements needed to selectively and potently inhibit SIRT2 deacetylase and decanoylase

Abstract

A high-quality X-ray crystal structure reveals the mechanism of compound 1a inhibiting SIRT2 deacetylase and decanoylase. Structure–activity relationship (SAR) analysis of the synthesized derivatives of 1a reveals the high requirements needed for selective inhibitors to bind with the induced hydrophobic pocket and potently inhibit sirtuin 2 deacetylase.

Graphical abstract: Crystallographic and SAR analyses reveal the high requirements needed to selectively and potently inhibit SIRT2 deacetylase and decanoylase

Supplementary files

Article information

Article type
Research Article
Submitted
13 Sep 2018
Accepted
06 Dec 2018
First published
07 Dec 2018

Med. Chem. Commun., 2019,10, 164-168

Crystallographic and SAR analyses reveal the high requirements needed to selectively and potently inhibit SIRT2 deacetylase and decanoylase

L. Yang, W. Xu, J. Yan, H. Su, C. Yuan, C. Li, X. Zhang, Z. Yu, Y. Yan, Y. Yu, Q. Chen, Z. Wang, L. Li, S. Qian and G. Li, Med. Chem. Commun., 2019, 10, 164 DOI: 10.1039/C8MD00462E

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