High-field NMR studies of molecular recognition and structure-function relationships in antimicrobial piscidins at the water-lipid bilayer interface.

Chekmenev EY, Jones SM, Nikolayeva YN, Vollmar BS, Wagner TJ, Gor'kov PL, Brey WW, Manion MN, Daugherty KC, Cotten M
J Am Chem Soc. 2006 128 (16): 5308-9

PMID: 16620079 · DOI:10.1021/ja058385e

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.

MeSH Terms (7)

Anti-Infective Agents Antimicrobial Cationic Peptides Fish Proteins Lipid Bilayers Nuclear Magnetic Resonance, Biomolecular Structure-Activity Relationship Water

Connections (1)

This publication is referenced by other Labnodes entities:

Links