Jump to main content
Jump to site search


Mercaptoacetate thioesters and their hydrolysate mercaptoacetic acid jointly inhibit Metallo-β-Lactamase L1

Abstract

The ‘superbug’ infection caused by metallo-β-lactamases (MβLs) including L1 has grown into an emerging threat. To probe a truth that mercaptoacetate thioester inhibiting L1 is contribution of the thioesteritself or its hydrolysate, ten mercaptoacetate thioesters 1-10 were synthesized, which specifically inhibited L1, exhibiting an IC50 ranging from 0.17 to 1.2 μM, and 8 was found to be the best inhibitor (IC50 = 0.17 μM). These thioesters restored 2-4-fold antimicrobial activity of cefazolin against E. coli expressing L1. UV-Vis monitoring shown that 1, 8 and 9 was unhydrolyzed in Tris buffer (pH 6.0-8.5), but hydrolyzed by L1, further HPLC monitoring indicated that 1/3 of the thioester 9 were converted to mercaptoacetic acid. STD-NMR monitoring suggested that both thioester and its hydrolysate mercaptoacetic acid jointly inhibited L1.

Back to tab navigation

Supplementary files

Publication details

The article was received on 16 Feb 2018, accepted on 04 May 2018 and first published on 17 May 2018


Article type: Research Article
DOI: 10.1039/C8MD00091C
Citation: Med. Chem. Commun., 2018, Accepted Manuscript
  •   Request permissions

    Mercaptoacetate thioesters and their hydrolysate mercaptoacetic acid jointly inhibit Metallo-β-Lactamase L1

    C. Chen, Y. Xiang, Y. Liu, X. Hu and K. Yang, Med. Chem. Commun., 2018, Accepted Manuscript , DOI: 10.1039/C8MD00091C

Search articles by author

Spotlight

Advertisements