B1CTcu5: A frog-derived brevinin-1 peptide with anti-tuberculosis activity.
Amphibian Proteins
/ chemical synthesis
Animals
Antimicrobial Cationic Peptides
/ chemical synthesis
Antitubercular Agents
/ pharmacology
Anura
/ physiology
Cells, Cultured
Humans
Macrophages
/ drug effects
Microbial Sensitivity Tests
/ methods
Mycobacterium tuberculosis
/ drug effects
Structure-Activity Relationship
Tuberculosis
/ drug therapy
B1CTcu5
Cationic antibacterial peptides
Macrophage
Mycobacterium tuberculosis
Journal
Peptides
ISSN: 1873-5169
Titre abrégé: Peptides
Pays: United States
ID NLM: 8008690
Informations de publication
Date de publication:
10 2020
10 2020
Historique:
received:
04
04
2020
revised:
12
07
2020
accepted:
13
07
2020
pubmed:
18
7
2020
medline:
20
7
2021
entrez:
18
7
2020
Statut:
ppublish
Résumé
Tuberculosis (TB) is a devastating infectious disease that causes a high rate of mortality. Drugs with new modes of action are needed to overcome this scenario. Cationic antibacterial peptides can serve as a potential alternative to existing TB drugs as they target the entire bacterial membrane for activity, thereby reducing the probability of development of drug resistance. In this study, we report anti-tuberculosis activity of B1CTcu5, a peptide that belongs to brevinin-1 family of antimicrobial peptides. This peptide possesses potent in vitro inhibitory activity against M. tuberculosis at 12.5 μg/mL but was not active against M. smegmatis. B1CTcu5 successfully eliminated intracellular mycobacteria without inducing cytotoxicity to the human macrophages at the concentrations tested. This peptide can be used as a template to design peptide-based anti-tubercular agents.
Identifiants
pubmed: 32679168
pii: S0196-9781(20)30122-4
doi: 10.1016/j.peptides.2020.170373
pii:
doi:
Substances chimiques
Amphibian Proteins
0
Antimicrobial Cationic Peptides
0
Antitubercular Agents
0
brevinin-1 protein, Rana
145963-49-1
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
170373Informations de copyright
Copyright © 2020 Elsevier Inc. All rights reserved.