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Binding of the Antimicrobial Peptide Temporin L to Liposomes Assessed by Trp Fluorescence
Journal of Biological Chemistry
The structure and membrane topology of the antimicrobial peptide temporin L (FVQWFSKFLGRIL-NH 2 ) were studied using liposomes as model bilayers. Circular dichroic spectra revealed temporin L to adopt an ␣-helical conformation when bound to liposomes. Binding of temporin L to liposomes induced significant blue shifts of the emission spectra of the single Trp residue (Trp 4 ) and also changed its quantum yield. The observed changes in the characteristics of the Trp 4 fluorescence are in keepingdoi:10.1074/jbc.m203186200 pmid:11991956 fatcat:temtjjaha5bupjhiuwwdy4qdg4