Original paper

Structure–Activity Relationship of the Antimicrobial Peptide Gomesin: The Role of Peptide Hydrophobicity in Its Interaction with Model Membranes

Volume: 30, Issue: 12, Pages: 3513 - 3521
Published: Mar 21, 2014
Abstract
Antimicrobial peptides are part of the innate immune system of animals and plants. Their lytic activity against microorganisms generally depends on their ability to disrupt and permeabilize membranes. Here we study the structure-activity relationship of the antimicrobial peptide gomesin (Gm), from the spider Acanthoscurria gomesiana, with large unilamellar vesicles (LUVs) composed of 3:7 palmitoyloleoyl phosphatidylglycerol: palmitoyloleoyl...
Paper Details
Title
Structure–Activity Relationship of the Antimicrobial Peptide Gomesin: The Role of Peptide Hydrophobicity in Its Interaction with Model Membranes
Published Date
Mar 21, 2014
Journal
Volume
30
Issue
12
Pages
3513 - 3521
Citation AnalysisPro
  • Scinapse’s Top 10 Citation Journals & Affiliations graph reveals the quality and authenticity of citations received by a paper.
  • Discover whether citations have been inflated due to self-citations, or if citations include institutional bias.