High-resolution structural profile of hylaseptin-4: Aggregation, membrane topology and pH dependence of overall membrane binding process.
Amino Acid Sequence
Animals
Antimicrobial Cationic Peptides
/ chemical synthesis
Anura
/ metabolism
Circular Dichroism
Escherichia coli
/ drug effects
Hydrogen-Ion Concentration
Liposomes
/ chemistry
Molecular Dynamics Simulation
Nuclear Magnetic Resonance, Biomolecular
Protein Binding
Protein Conformation, alpha-Helical
Staphylococcus aureus
/ drug effects
Aggregation process
Antimicrobial mechanism of action
Biophysical prediction of peptidemembrane interactions
Conformational analysis of peptides
Membrane active peptides
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 05 2021
01 05 2021
Historique:
received:
11
11
2020
revised:
20
01
2021
accepted:
03
02
2021
pubmed:
9
2
2021
medline:
9
9
2021
entrez:
8
2
2021
Statut:
ppublish
Résumé
Hylaseptin-4 (HSP-4, GIGDILKNLAKAAGKAALHAVGESL-NH
Identifiants
pubmed: 33556358
pii: S0005-2736(21)00032-8
doi: 10.1016/j.bbamem.2021.183581
pii:
doi:
Substances chimiques
Antimicrobial Cationic Peptides
0
Liposomes
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
183581Informations de copyright
Copyright © 2021 Elsevier B.V. All rights reserved.