Issue 6, 2007

Nε-Methanesulfonyl-lysine as a non-hydrolyzable functional surrogate for Nε-acetyl-lysine

Abstract

Through parallel studies on peptides containing Nε-methanesulfonyl-lysine or Nε-acetyl-lysine, Nε-methanesulfonyl-lysine as a replacement for Nε-acetyl-lysine was shown i) not to compromise the binding affinity for a bromodomain, ii) to confer resistance to human HDAC8 and SIRT1 (two distinct protein deacetylases), and iii) to confer only weak inhibition against human HDAC8 and SIRT1. These results suggested Nε-methanesulfonyl-lysine as a non-hydrolyzable functional surrogate for Nε-acetyl-lysine.

Graphical abstract: N ε-Methanesulfonyl-lysine as a non-hydrolyzable functional surrogate for Nε-acetyl-lysine

Supplementary files

Article information

Article type
Communication
Submitted
24 Nov 2006
Accepted
25 Jan 2007
First published
05 Feb 2007

Org. Biomol. Chem., 2007,5, 892-896

N ε-Methanesulfonyl-lysine as a non-hydrolyzable functional surrogate for Nε-acetyl-lysine

N. Jamonnak, D. G. Fatkins, L. Wei and W. Zheng, Org. Biomol. Chem., 2007, 5, 892 DOI: 10.1039/B617185K

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