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Peptide‐related alterations of membrane‐associated water: deuterium solid‐state NMR investigations of phosphatidylcholine membranes at different hydration levels
Author(s) -
Mendonça Moraes Cléria,
Bechinger Burkhard
Publication year - 2004
Publication title -
magnetic resonance in chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.483
H-Index - 72
eISSN - 1097-458X
pISSN - 0749-1581
DOI - 10.1002/mrc.1321
Subject(s) - chemistry , popc , deuterium nmr , membrane , bilayer , deuterium , peptide , solid state nuclear magnetic resonance , phospholipid , lipid bilayer , phosphatidylcholine , nuclear magnetic resonance spectroscopy , chromatography , crystallography , analytical chemistry (journal) , stereochemistry , nuclear magnetic resonance , biochemistry , physics , quantum mechanics
Deuterated water associated with oriented POPC bilayers was investigated before and after the addition of 2 mol% peptide. Membranes in the presences of antimicrobial‐(LAH4), pore‐forming‐ (the segments M2 of influenza A and S4 of the domain I of rat brain sodium channels) or lysine‐containing model peptides (LAK1 and LAK3) were investigated by 2 H and proton‐decoupled 31 P solid‐state NMR. The NMR spectra were recorded as a function of hydration in the range between 15 and 93% relative humidity and of sample composition. In the presence of peptides an increased association of water is observed. A quantitative analysis suggests that the peptide‐induced changes in the lipid bilayer packing have a significant effect on membrane–water association. The quadrupolar splittings of 2 H 2 O at a given degree of hydration indicate that the changes of the water deuterium order parameter are specific for the peptide sequence and the lipid composition. Copyright © 2004 John Wiley & Sons, Ltd.