Ribosomal Target-Binding Sites of Antimicrobial Peptides Api137 and Onc112 Are Conserved among Pathogens Indicating New Lead Structures To Develop Novel Broad-Spectrum Antibiotics.
Acinetobacter baumannii
/ drug effects
Anti-Bacterial Agents
/ chemistry
Binding Sites
/ drug effects
Escherichia coli
/ chemistry
Klebsiella pneumoniae
/ drug effects
Microbial Sensitivity Tests
Molecular Structure
Pore Forming Cytotoxic Proteins
/ chemistry
Pseudomonas aeruginosa
/ drug effects
Ribosomes
/ drug effects
Staphylococcus aureus
/ drug effects
70S ribosome
antimicrobial peptides
apidaecin
fluorescein polarization
oncocin
Journal
Chembiochem : a European journal of chemical biology
ISSN: 1439-7633
Titre abrégé: Chembiochem
Pays: Germany
ID NLM: 100937360
Informations de publication
Date de publication:
14 09 2020
14 09 2020
Historique:
received:
25
02
2020
pubmed:
16
4
2020
medline:
8
7
2021
entrez:
16
4
2020
Statut:
ppublish
Résumé
Proline-rich antimicrobial peptides expressed in insects are primarily active against Enterobacteriaceae. Mechanistically, they target the bacterial (70S) ribosome after partially transporter-based cellular uptake, as revealed for Api137 and Onc112 on Escherichia coli. Following molecular modeling indicating that the Onc112 contact site is conserved among the ribosomes of high-priority pathogens, the ribosome binding of Api137 and Onc112 was studied. The dissociation constants (K
Identifiants
pubmed: 32293093
doi: 10.1002/cbic.202000109
pmc: PMC7540576
doi:
Substances chimiques
Anti-Bacterial Agents
0
Pore Forming Cytotoxic Proteins
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
2628-2634Informations de copyright
© 2020 The Authors. Published by Wiley-VCH Verlag GmbH & Co. KGaA.
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