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Identification and characterization of novel sirtuin inhibitor scaffolds.

Abstract：

:The sirtuin proteins are broadly conserved NAD(+)-dependent deacetylases that are implicated in diverse biological processes including DNA recombination and repair, transcriptional silencing, longevity, apoptosis, axonal protection, insulin signaling, and fat mobilization. Because of these associations, the identification of small molecule sirtuin modulators has been of significant interest. Here we report on high throughput screening against the yeast sirtuin, Hst2, leading to the identification of four unique inhibitor scaffolds that also inhibit the human sirtuins, SIRT1-3, and are able to inhibit telomeric silencing of yeast Sir2 in vivo. The identified inhibitor scaffolds range in potency from IC(50) values of 6.5-130 microM against Hst2. Each of the inhibitor scaffolds binds reversibly to the enzyme, and kinetic analysis reveals that each of the inhibitors is non-competitive with respect to both acetyl-lysine and NAD(+) binding. Limited SAR analysis of the scaffolds also identifies which functional groups may be important for inhibition. These sirtuin inhibitors are low molecular weight and well-suited for lead molecule optimization, making them useful chemical probes to study the mechanism and biological roles of sirtuins and potential starting points for optimization into therapeutics.

journal_name

Bioorg Med Chem

journal_title

Bioorganic & medicinal chemistry

authors

Sanders BD,Jackson B,Brent M,Taylor AM,Dang W,Berger SL,Schreiber SL,Howitz K,Marmorstein R

doi

10.1016/j.bmc.2009.07.073

subject

Has Abstract

pub_date

2009-10-01 00:00:00

pages

7031-41

issue

19

eissn

0968-0896

issn

1464-3391

pii

S0968-0896(09)00724-X

journal_volume

17

pub_type

杂志文章

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