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Mechanism-based inhibitors of SIRT2: structure-activity relationship, X-ray structures, target engagement, regulation of α-tubulin acetylation and inhibition of breast cancer cell migration.

RSC chemical biology (2021-08-31)
Alexander L Nielsen, Nima Rajabi, Norio Kudo, Kathrine Lundø, Carlos Moreno-Yruela, Michael Bæk, Martin Fontenas, Alessia Lucidi, Andreas S Madsen, Minoru Yoshida, Christian A Olsen
ABSTRACT

Sirtuin 2 (SIRT2) is a protein deacylase enzyme that removes acetyl groups and longer chain acyl groups from post-translationally modified lysine residues. It affects diverse biological functions in the cell and has been considered a drug target in relation to both neurodegenerative diseases and cancer. Therefore, access to well-characterized and robust tool compounds is essential for the continued investigation of the complex functions of this enzyme. Here, we report a collection of chemical probes that are potent, selective, stable in serum, water-soluble, and inhibit SIRT2-mediated deacetylation and demyristoylation in cells. Compared to the current landscape of SIRT2 inhibitors, this is a unique ensemble of features built into a single compound. We expect the developed chemotypes to find broad application in the interrogation of SIRT2 functions in both healthy and diseased cells, and to provide a foundation for the development of future therapeutics.

MATERIALS
Product Number
Brand
Product Description

Roche
不含EDTA的cOmplete蛋白酶抑制剂混合物, Tablets provided in glass vials
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