substituting nε-thioacetyl-lysine for nε-acetyl-lysine in peptide substrates as a general approach to inhibiting human nad+-dependent protein deacetylases替换为nε-acetyl-lysine nε-thioacetyl-lysine肽基板作为一般人类nad +端依赖蛋白去乙酰酶抑制剂抑制方法.pdfVIP

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substituting nε-thioacetyl-lysine for nε-acetyl-lysine in peptide substrates as a general approach to inhibiting human nad+-dependent protein deacetylases替换为nε-acetyl-lysine nε-thioacetyl-lysine肽基板作为一般人类nad +端依赖蛋白去乙酰酶抑制剂抑制方法.pdf

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substitutingnε-thioacetyl-lysinefornε-acetyl-lysineinpeptidesubstratesasageneralapproachtoinhibitinghumannad-dependentproteindeacetylases替换为nε-acetyl-lysinenε-thioacetyl-lysine肽基板作为一般人类nad端依赖蛋白去乙酰酶抑制剂抑制方法

Int. J. Mol. Sci. 2008, 9, 1-11 International Journal of Molecular Sciences ISSN 1422-0067 © 2008 by MDPI /ijms Full Research Paper ε ε Substituting N -thioacetyl-lysine for N -acetyl-lysine in Peptide Substrates as a General Approach to Inhibiting Human NAD+-dependent Protein Deacetylases David G. Fatkins and Weiping Zheng * Department of Chemistry, University of Akron, 190 E. Buchtel Commons, Akron, OH 44325, USA; E-mail: dfatkins03@; wzheng@ * Author to whom correspondence should be addressed; E-mail: wzheng@ Received: 12 November 2007; in revised form: 21 December 2007 / Accepted: 2 January 2008 / Published: 7 January 2008 + Abstract: Inhibitors of human NAD -dependent protein deacetylases possess great value for deciphering the biology of these enzymes and as potential therapeutics for metabolic and age- related diseases and cancer. In the current study, we have experimentally demonstrated that, the potent inhibition we obtained previously for one of these enzymes (i.e. sirtuin type 1 (SIRT1)) ε ε by simply replacing N -thioacetyl-lysine for N -acetyl-lysine in its peptide substrate, represented a general and efficient strategy to develop potent and selective inhibitors of human + NAD -dependent protein deacetylase