19F NMR analysis of the antimicrobial peptide PGLa bound to native cell membranes from bacterial protoplasts and human erythrocytes.
(19)F NMR is a unique tool to examine the structure of fluorine-labeled peptides in their native cellular environment, due to an exquisite sensitivity and lack of natural abundance background. For solid-state NMR analysis, we isolated native membranes from erythrocyte ghosts and bacterial protoplasts and prepared them as macroscopically oriented samples. They showed a high purity and quality of alignment according to (31)P NMR, and the membrane-bound antimicrobial peptide PGLa could be detected by (19)F NMR. The characteristic fingerprint splitting of its (19)F reporter group indicated that the peptide helix binds to the native membranes in a surface alignment, albeit with a higher affinity in the prokaryotic than the eukaryotic system.
Ieronimo
Marco
M
Institute of Organic Chemistry and DFG-Center for Functional Nanostructures, Karlsruhe Institute of Technology, Fritz-Haber-Weg 6, 76131 Karlsruhe, Germany.
Afonin
Sergii
S
Koch
Katja
K
Berditsch
Marina
M
Wadhwani
Parvesh
P
Ulrich
Anne S
AS
D000595:Amino Acid Sequence; D000818:Animals; D023181:Antimicrobial Cationic Peptides / Q000737:chemistry* / Q000378:metabolism*; D001419:Bacteria / Q000166:cytology*; D002462:Cell Membrane / Q000378:metabolism*; D004912:Erythrocytes / Q000166:cytology*; D019617:Halobacterium salinarum / Q000166:cytology; D006801:Humans; D009682:Magnetic Resonance Spectroscopy; D016982:Micrococcus luteus / Q000166:cytology; D008969:Molecular Sequence Data; D011523:Protoplasts / Q000166:cytology*; D014982:Xenopus laevis
D023181:Antimicrobial Cationic Peptides; C045866:peptide-Gly-Leu-amide