학술논문
Temperature-Dependent Transmembrane Insertion of the Amphiphilic Peptide PGLa in Lipid Bilayers Observed by Solid State [sup19]F NMR Spectroscopy.
Document Type
Article
Source
Subject
*ANTIMICROBIAL peptides
*BILAYER lipid membranes
*BIOLOGICAL membranes
*SPECTRUM analysis
*LIPIDS
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Language
ISSN
0002-7863
Abstract
The article presents a study on the membrane-alignment of the -helical amphiphilic antimicrobial peptide PGLa in DMPC/DMPG bilayers by utilizing solid state 19F NMR spectroscopy. It shows that the helix alignment depends not just on peptide concentration but also with temperature and lipid phase state. It reveals three distinct states of alignment that have been discovered for PGLa in lipid bilayers.