Proline Hinged Amphipathic α-Helical Peptide Sensitizes Gram-Negative Bacteria to Various Gram-Positive Antibiotics.
Animals
Anti-Bacterial Agents
/ chemistry
Antimicrobial Cationic Peptides
/ chemistry
Cell Membrane
/ drug effects
Clarithromycin
/ pharmacology
Escherichia coli
/ drug effects
Female
Hemolysis
/ drug effects
Humans
Hydrophobic and Hydrophilic Interactions
Linezolid
/ pharmacology
Lipid A
/ metabolism
Membrane Fluidity
/ drug effects
Mice, Inbred ICR
Microbial Sensitivity Tests
Proline
/ chemistry
Protein Binding
Protein Conformation, alpha-Helical
Rifampin
/ pharmacology
Journal
Journal of medicinal chemistry
ISSN: 1520-4804
Titre abrégé: J Med Chem
Pays: United States
ID NLM: 9716531
Informations de publication
Date de publication:
10 12 2020
10 12 2020
Historique:
pubmed:
19
11
2020
medline:
4
2
2021
entrez:
18
11
2020
Statut:
ppublish
Résumé
Gram-negative bacteria are becoming resistant to almost all currently available antibiotics. Systemically designed antimicrobial peptides (AMPs) are attractive agents to enhance the activities of antibiotics. We constructed a small Pro-scanning library using amphipathic model peptides. Measurements of minimum inhibitory concentration (MIC) against
Identifiants
pubmed: 33205989
doi: 10.1021/acs.jmedchem.0c01506
doi:
Substances chimiques
Anti-Bacterial Agents
0
Antimicrobial Cationic Peptides
0
Lipid A
0
Proline
9DLQ4CIU6V
Clarithromycin
H1250JIK0A
Linezolid
ISQ9I6J12J
Rifampin
VJT6J7R4TR
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM