Inhibition of bacterial and human zinc-metalloproteases by bisphosphonate- and catechol-containing compounds.

ABSTRACT: Compounds containg catechol or bisphosphonate were tested as inhibitors of the zinc metalloproteases, thermolysin (TLN), pseudolysin (PLN) and aureolysin (ALN) which are bacterial virulence factors, and the human matrix metalloproteases MMP-9 and -14. Inhibition of virulence is a putative strategy in the development of antibacterial drugs, but the inhibitors should not interfere with human enzymes. Docking indicated that the inhibitors bound MMP-9 and MMP-14 with the phenyl, biphenyl, chlorophenyl, nitrophenyl or methoxyphenyl ringsystem in the S₁'-subpocket, while these ringsystems entered the S₂'- or S₁ -subpockets or a region involving amino acids in the S₁'- and S₂'-subpockets of the bacterial enzymes. An arginine conserved among t

SUBMITTER: Rahman F 

PROVIDER: S-EPMC7993378 | biostudies-literature | 2021 Dec

REPOSITORIES: biostudies-literature