High-field NMR studies of molecular recognition and structure-function relationships in antimicrobial piscidins at the water-lipid bilayer interface.
High magnetic field solid-state NMR was performed on amphipathic cationic antimicrobial peptides from fish to characterize their secondary structure and orientation in hydrated phospholipid bilayers. High-resolution distance and orientational restraints on 13C- and 15N-labeled amidated piscidins 1 and 3 provided site-specific information establishing alpha-helicity and an orientation parallel to the membrane surface. Few membrane-bound natural peptides with this topology have been structurally studied at high resolution in the presence of hydrated lipid bilayers. This orientation was foreseen since the partitioning of amphipathic cationic antimicrobial peptides at the water-bilayer interface allows for favorable peptide-lipid interactions, and it may be related to the mechanism of action. The enhanced resolution obtained at 900 MHz evidences a determinant advantage of ultra-high-field NMR for the structural determination of multiple-labeled peptides and proteins.
Chekmenev
Eduard Y
EY
Center for Interdisciplinary Magnetic Resonance, National High Magnetic Field Laboratory, 1800 East Paul Dirac Drive, Tallahassee, Florida 32310, USA.
Jones
Shiela M
SM
Nikolayeva
Yelena N
YN
Vollmar
Breanna S
BS
Wagner
Tim J
TJ
Gor'kov
Peter L
PL
Brey
William W
WW
Manion
McKenna N
MN
Daugherty
Ken C
KC
Cotten
Myriam
M
D000890:Anti-Infective Agents / Q000737:chemistry* / Q000494:pharmacology; D023181:Antimicrobial Cationic Peptides / Q000737:chemistry* / Q000494:pharmacology*; D029941:Fish Proteins / Q000737:chemistry* / Q000494:pharmacology*; D008051:Lipid Bilayers; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D013329:Structure-Activity Relationship; D014867:Water / Q000737:chemistry*
D000890:Anti-Infective Agents; D023181:Antimicrobial Cationic Peptides; D029941:Fish Proteins; D008051:Lipid Bilayers; C449802:moronecidin protein, Morone saxatilis; D014867:Water