Folding profiles of antimicrobial scorpion venom-derived peptides on hydrophobic surfaces: a molecular dynamics study.
Scorpion derived-peptides
antimicrobial peptides
molecular dynamics
peptide folding
Journal
Journal of biomolecular structure & dynamics
ISSN: 1538-0254
Titre abrégé: J Biomol Struct Dyn
Pays: England
ID NLM: 8404176
Informations de publication
Date de publication:
Jul 2020
Jul 2020
Historique:
pubmed:
28
7
2019
medline:
22
6
2021
entrez:
27
7
2019
Statut:
ppublish
Résumé
Most helical antimicrobial peptides (AMPs) are usually unfolded in aqueous solution; however they acquire their secondary structure in the presence of a hydrophobic environment such as lipid membranes. Being the biological membranes the main target of many AMPs it is necessary to understand their way of action. Pandinin 2 (Pin2) is an alpha-helical AMP isolated from the venom of the African scorpion
Identifiants
pubmed: 31345123
doi: 10.1080/07391102.2019.1648319
doi:
Substances chimiques
Anti-Bacterial Agents
0
Anti-Infective Agents
0
Antimicrobial Cationic Peptides
0
Scorpion Venoms
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM