Membrane interactions of the anuran antimicrobial peptide HSP1-NH
Antimicrobial mechanism of action
Antimicrobial peptides
Biophysical prediction of peptide-membrane interactions
Conformational analysis of peptides
Membrane active peptides
Membrane-dependent composition
Peptide-membrane interaction
Journal
Biochimica et biophysica acta. Biomembranes
ISSN: 1879-2642
Titre abrégé: Biochim Biophys Acta Biomembr
Pays: Netherlands
ID NLM: 101731713
Informations de publication
Date de publication:
01 01 2021
01 01 2021
Historique:
received:
28
04
2020
revised:
08
08
2020
accepted:
17
08
2020
pubmed:
24
8
2020
medline:
13
4
2021
entrez:
24
8
2020
Statut:
ppublish
Résumé
Studies have suggested that antimicrobial peptides act by different mechanisms, such as micellisation, self-assembly of nanostructures and pore formation on the membrane surface. This work presents an extensive investigation of the membrane interactions of the 14 amino-acid antimicrobial peptide hylaseptin P1-NH
Identifiants
pubmed: 32828849
pii: S0005-2736(20)30292-3
doi: 10.1016/j.bbamem.2020.183449
pii:
doi:
Substances chimiques
Amphibian Proteins
0
Membranes, Artificial
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
183449Informations de copyright
Copyright © 2020 Elsevier B.V. All rights reserved.