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

Sanders, M. R., Clifton, L. A., Frazier, R. A. and Green, R. J. (2017) Tryptophan to arginine substitution in puroindoline b alters binding to model eukaryotic membranes. Langmuir, 33 (19). pp. 4847-4853. ISSN 0743-7463

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To link to this item DOI: 10.1021/acs.langmuir.6b03030

Abstract/Summary

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.

Item Type:Article
Refereed:Yes
Divisions:Faculty of Life Sciences > School of Chemistry, Food and Pharmacy > School of Pharmacy > Pharmaceutics Research Group
Faculty of Life Sciences > School of Chemistry, Food and Pharmacy > Department of Food and Nutritional Sciences > Food Research Group
ID Code:70863
Publisher:American Chemical Society

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