Crystallographic and SAR analyses reveal the high requirements needed to selectively and potently inhibit SIRT2 deacetylase and decanoylase.
Ling-Ling YangWei XuJie YanHui-Lin SuChen YuanChao LiXing ZhangZhu-Jun YuYu-Hang YanYamei YuQiang ChenZhouyu WangLin LiShan QianGuo-Bo LiPublished in: MedChemComm (2018)
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.