Epimers l- and d-Phenylseptin: How the relative stereochemistry affects the peptide-membrane interactions.
Antimicrobial mechanism of action
Biophysical prediction of peptide-membrane interactions
Conformational analysis of peptides
L and D peptide epimers
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 11 2021
01 11 2021
Historique:
received:
18
04
2021
revised:
15
07
2021
accepted:
19
07
2021
pubmed:
27
7
2021
medline:
18
11
2021
entrez:
26
7
2021
Statut:
ppublish
Résumé
In recent decades, several epimers of peptides containing d-amino acids have been identified in antimicrobial sequences, a feature which has been associated with post-translational modification. Generally, d-isomers present similar or inferior antimicrobial activity, only surpassing their epimers in resistance to peptidases. The naturally occurring l-Phenylseptin (l-Phes) and d-Phenylseptin (d-Phes) peptides (FFFDTLKNLAGKVIGALT-nh
Identifiants
pubmed: 34310911
pii: S0005-2736(21)00157-7
doi: 10.1016/j.bbamem.2021.183708
pii:
doi:
Substances chimiques
Peptides
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
183708Informations de copyright
Copyright © 2021. Published by Elsevier B.V.