Antifungal evaluation and mechanistic investigations of membrane active short synthetic peptides-based amphiphiles.
Antifungal peptides
C. neoformans
Membrane disruption
N-1-Benzyl-l-histidine
Peptide-based antibiotics
Pore formation
Journal
Bioorganic chemistry
ISSN: 1090-2120
Titre abrégé: Bioorg Chem
Pays: United States
ID NLM: 1303703
Informations de publication
Date de publication:
10 2022
10 2022
Historique:
received:
25
05
2022
revised:
28
06
2022
accepted:
30
06
2022
pubmed:
12
7
2022
medline:
16
8
2022
entrez:
11
7
2022
Statut:
ppublish
Résumé
The quest for new class of peptide-based antibiotics has steered this research towards the design and synthesis of short sequences possessing modified amphiphilic histidine along with hydrophobic tryptophan residues. The new structural class of dipeptides Trp-His(1-Bn)-OMe/NHBn and tripeptides His(1-Bn)-Trp-His(1-Bn)-OMe/NHBn demonstrated promising antifungal and antibacterial activities with membrane lytic action. The illustration of desirable hydrophilic-lipophilic balance appeared in the dipeptide Trp-His[1-(3,5-di-tert-butylbenzyl)]-NHBn (13d) that produced the most promising antifungal activity with IC
Identifiants
pubmed: 35816873
pii: S0045-2068(22)00408-4
doi: 10.1016/j.bioorg.2022.106002
pii:
doi:
Substances chimiques
Anti-Bacterial Agents
0
Antifungal Agents
0
Dipeptides
0
Peptides
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
106002Informations de copyright
Copyright © 2022 Elsevier Inc. All rights reserved.