학술논문

[Super 19]F NMR analysis of the antimicrobial peptide PGLa bound to native cell membranes from bacterial protoplasts and human erythrocytes
Document Type
Report
Source
Journal of the American Chemical Society. July 7, 2010, Vol. 132 Issue 26, 8822-8824
Subject
Anti-infective agents -- Structure
Anti-infective agents -- Chemical properties
Membrane proteins -- Structure
Membrane proteins -- Chemical properties
Nuclear magnetic resonance spectroscopy -- Usage
Chemistry
Language
English
ISSN
0002-7863
Abstract
[Super 19]F NMR solid-state analysis was performed to isolate native membranes from erythrocyte ghosts and bacterial protoplasts and prepare them as macroscopically oriented samples. The characteristic fingerprint splitting of the membrane-bound antimicrobial peptide PGLa detected by [super 19]F reporter group indicated that the peptide helix binds to the native membranes in a surface alignment, although with a higher affinity in the prokaryotic than the eukaryotic system.