Bacterial Aggregation Triggered by Fibril Forming Tryptophan-Rich Sequences: Effects of Peptide Side Chain and Membrane Phospholipids.
antimicrobial peptide
bacterial aggregation
fibrillar structure
fluorescence resonance energy transfer
liposome aggregation
Journal
ACS applied materials & interfaces
ISSN: 1944-8252
Titre abrégé: ACS Appl Mater Interfaces
Pays: United States
ID NLM: 101504991
Informations de publication
Date de publication:
17 Jun 2020
17 Jun 2020
Historique:
pubmed:
19
5
2020
medline:
2
3
2021
entrez:
19
5
2020
Statut:
ppublish
Résumé
The influence of side chain residue and phospholipid characteristics of the cytoplasmic membrane upon the fibrillation and bacterial aggregation of arginine (Arg) and tryptophan (Trp) rich antimicrobial peptides (AMPs) has not been well described to date. Here, we utilized the structural advantages of HHC-10 and
Identifiants
pubmed: 32422035
doi: 10.1021/acsami.0c04336
doi:
Substances chimiques
Antimicrobial Cationic Peptides
0
Liposomes
0
Peptides
0
Phospholipids
0
Tryptophan
8DUH1N11BX
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM