N(epsilon)-methanesulfonyl-lysine as a non-hydrolyzable functional surrogate for N(epsilon)-acetyl-lysine.
Through parallel studies on peptides containing N(epsilon)-methanesulfonyl-lysine or N(epsilon)-acetyl-lysine, N(epsilon)-methanesulfonyl-lysine as a replacement for N(epsilon)-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 N(epsilon)-methanesulfonyl-lysine as a non-hydrolyzable functional surrogate for N(epsilon)-acetyl-lysine.
Jamonnak
Nuttara
N
Department of Chemistry, University of Akron, 190 E. Buchtel Commons, Akron, OH 44325, USA.
Fatkins
David G
DG
Wei
Lanlan
L
Zheng
Weiping
W
D002851:Chromatography, High Pressure Liquid; D006655:Histone Deacetylases / Q000378:metabolism; D006801:Humans; D006868:Hydrolysis; D008239:Lysine / Q000031:analogs & derivatives* / Q000138:chemical synthesis / Q000737:chemistry / Q000378:metabolism*; D010455:Peptides; D012097:Repressor Proteins / Q000378:metabolism; D056564:Sirtuin 1; D037761:Sirtuins / Q000378:metabolism
C520584:N-epsilon-methanesulfonyllysine; D010455:Peptides; D012097:Repressor Proteins; C016949:N-epsilon-acetyllysine; C447939:SIRT1 protein, human; D056564:Sirtuin 1; D037761:Sirtuins; C409470:HDAC8 protein, human; D006655:Histone Deacetylases; D008239:Lysine