Folding profiles of antimicrobial scorpion venom-derived peptides on hydrophobic surfaces: a molecular dynamics study.


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
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

Pagination

2928-2938

Auteurs

José-Luis Velasco-Bolom (JL)

Instituto de Ciencias Físicas, Universidad Nacional Autónoma de México, Cuernavaca, Morelos, México.

Gerardo Corzo (G)

Departamento de Medicina Molecular y Bioprocesos, Instituto de Biotecnología, Universidad Nacional Autónoma de México, Cuernavaca, Morelos, México.

Ramón Garduño-Juárez (R)

Instituto de Ciencias Físicas, Universidad Nacional Autónoma de México, Cuernavaca, Morelos, México.

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Classifications MeSH