Inhibition of bacterial and human zinc-metalloproteases by bisphosphonate- and catechol-containing compounds.
Anti-Bacterial Agents
/ chemical synthesis
Bacteria
/ enzymology
Catechols
/ chemical synthesis
Diphosphonates
/ chemical synthesis
Humans
Matrix Metalloproteinase Inhibitors
/ chemical synthesis
Metalloendopeptidases
/ antagonists & inhibitors
Microbial Sensitivity Tests
Models, Molecular
Molecular Structure
THP-1 Cells
Zinc proteases
bacterial virulence factors
docking and scoring
enzyme inhibition
matrix metalloproteases
Journal
Journal of enzyme inhibition and medicinal chemistry
ISSN: 1475-6374
Titre abrégé: J Enzyme Inhib Med Chem
Pays: England
ID NLM: 101150203
Informations de publication
Date de publication:
Dec 2021
Dec 2021
Historique:
entrez:
24
3
2021
pubmed:
25
3
2021
medline:
17
7
2021
Statut:
ppublish
Résumé
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 S
Identifiants
pubmed: 33757387
doi: 10.1080/14756366.2021.1901088
pmc: PMC7993378
doi:
Substances chimiques
Anti-Bacterial Agents
0
Catechols
0
Diphosphonates
0
Matrix Metalloproteinase Inhibitors
0
Metalloendopeptidases
EC 3.4.24.-
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
819-830Références
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