Tryptophan to arginine substitution in puroindoline b alters binding to model eukaryotic membranes

Autor: Sanders, Michael R, Clifton, Luke A, Frazier, Richard A., Green, Rebecca J.
Jazyk: angličtina
Rok vydání: 2017
Předmět:
ISSN: 0743-7463
Popis: We have studied how puroindoline-b (PINB) mutants bind to model eukaryotic membranes dependent on binary composition of anionic:zwitterionic phospholipids and the presence of cholesterol and sphingomyelin in the model membrane. We have found that the trends in lipid binding behavior are different for wild-type PINB compared to its naturally occurring PINB(Trp44Arg) mutant form and have seen evidence of protein-induced domain formation within the lipid layer structure. Results show that selective binding of antimicrobial peptides to different membrane types is as a result of differences in lipid composition and the arrangement of lipids within the membrane surface. However, membrane-binding behavior is not easily predicted; it is determined by net charge, hydrophobicity, and the amphiphilicity of the protein/peptide lipid-binding domain.
Databáze: OpenAIRE