Effect of positive charges in the structural interaction of crabrolin isoforms with lipopolysaccharide.
NMR spectroscopy
antimicrobial peptides
crabrolin
lipopolysaccharide
Journal
Journal of peptide science : an official publication of the European Peptide Society
ISSN: 1099-1387
Titre abrégé: J Pept Sci
Pays: England
ID NLM: 9506309
Informations de publication
Date de publication:
Sep 2020
Sep 2020
Historique:
received:
15
02
2020
revised:
19
05
2020
accepted:
02
06
2020
pubmed:
26
6
2020
medline:
5
6
2021
entrez:
26
6
2020
Statut:
ppublish
Résumé
Antimicrobial peptides (AMPs) appear as chemical compounds of increasing interest for their role in killing bacteria and, more recently, for their ability to bind endotoxin (lipopolysaccharide, LPS) that is released during bacterial infection and that may lead to septic shock. This dual role in the mechanism of action can further be enhanced in a synergistic way when two or more AMPs are combined together. Not all AMPs are able to bind LPS, suggesting that several modes of binding to the bacterial surface may exist. Here we analyze a natural AMP, crabrolin, and two mutated forms, one with increased positive charge (Crabrolin Plus) and the other with null charge (Crabrolin Minus), and compare their binding abilities to LPS. While Crabrolin WT as well Crabrolin Minus do not show binding to LPS, the mutated Crabrolin Plus exhibits binding and forms a well defined structure in the presence of LPS. The results strengthen the importance of positive charges for the binding to LPS and suggest the mutated form with increased positive charge as a promising candidate for antimicrobial and antiseptic activity.
Substances chimiques
Antimicrobial Cationic Peptides
0
Lipopolysaccharides
0
Wasp Venoms
0
crabrolin
93207-22-8
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
e3271Subventions
Organisme : Horizon 2020 program of the European Union
ID : 653706
Informations de copyright
© 2020 European Peptide Society and John Wiley & Sons, Ltd.
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