skip to main content
OSTI.GOV title logo U.S. Department of Energy
Office of Scientific and Technical Information

Title: High-Field NMR Studies of Molecular Recognition and Structure-Function Relationships in Antimicrobial Piscidins at the Water-Lipid Bilayer Interface

Abstract

Piscidins are the first amphipathic, cationic, antimicrobial peptides (ACAPs) to be found in the mast cells of fish, and they are believed to play a crucial role in the fight against many aquatic infections.1 Many ACAPs have been characterized functionally, and some models for their mechanism of action exist, including the barrel-stave model, the wormhole model, the carpet mechanism, and the intracellular activation of fatal pathways.2-9 Much information remains to be learned about the details of their structure, initial interactions with membranes, and the ultimate mechanism for disrupting cellular function. To this end, we employed solid-state NMR (ssNMR) to probe the structure and topology of isotopically labeled piscidins in the membrane-bound state.

Authors:
; ; ; ; ; ; ; ; ;
Publication Date:
Research Org.:
Pacific Northwest National Laboratory (PNNL), Richland, WA (US), Environmental Molecular Sciences Laboratory (EMSL)
Sponsoring Org.:
USDOE
OSTI Identifier:
889058
DOE Contract Number:  
AC05-76RL01830
Resource Type:
Journal Article
Resource Relation:
Journal Name: Journal of the American Chemical Society; Journal Volume: 128; Journal Issue: 16
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; FISHES; MAST CELLS; MEMBRANES; TOPOLOGY; MORPHOLOGY; STRUCTURE-ACTIVITY RELATIONSHIPS; PEPTIDES; NUCLEAR MAGNETIC RESONANCE; Environmental Molecular Sciences Laboratory

Citation Formats

Chekmenev, Eduard Y., Jones, Shiela M., Nikolayeva, Yelena, Vollmar, Breanna S., Wagner, Timothy J., Gorkov, Peter L., Brey, William W., Manion, Mckenna N., Daugherty, Kenneth C., and Cotten, Myriam L. High-Field NMR Studies of Molecular Recognition and Structure-Function Relationships in Antimicrobial Piscidins at the Water-Lipid Bilayer Interface. United States: N. p., 2006. Web. doi:10.1021/ja058385e.
Chekmenev, Eduard Y., Jones, Shiela M., Nikolayeva, Yelena, Vollmar, Breanna S., Wagner, Timothy J., Gorkov, Peter L., Brey, William W., Manion, Mckenna N., Daugherty, Kenneth C., & Cotten, Myriam L. High-Field NMR Studies of Molecular Recognition and Structure-Function Relationships in Antimicrobial Piscidins at the Water-Lipid Bilayer Interface. United States. doi:10.1021/ja058385e.
Chekmenev, Eduard Y., Jones, Shiela M., Nikolayeva, Yelena, Vollmar, Breanna S., Wagner, Timothy J., Gorkov, Peter L., Brey, William W., Manion, Mckenna N., Daugherty, Kenneth C., and Cotten, Myriam L. Wed . "High-Field NMR Studies of Molecular Recognition and Structure-Function Relationships in Antimicrobial Piscidins at the Water-Lipid Bilayer Interface". United States. doi:10.1021/ja058385e.
@article{osti_889058,
title = {High-Field NMR Studies of Molecular Recognition and Structure-Function Relationships in Antimicrobial Piscidins at the Water-Lipid Bilayer Interface},
author = {Chekmenev, Eduard Y. and Jones, Shiela M. and Nikolayeva, Yelena and Vollmar, Breanna S. and Wagner, Timothy J. and Gorkov, Peter L. and Brey, William W. and Manion, Mckenna N. and Daugherty, Kenneth C. and Cotten, Myriam L.},
abstractNote = {Piscidins are the first amphipathic, cationic, antimicrobial peptides (ACAPs) to be found in the mast cells of fish, and they are believed to play a crucial role in the fight against many aquatic infections.1 Many ACAPs have been characterized functionally, and some models for their mechanism of action exist, including the barrel-stave model, the wormhole model, the carpet mechanism, and the intracellular activation of fatal pathways.2-9 Much information remains to be learned about the details of their structure, initial interactions with membranes, and the ultimate mechanism for disrupting cellular function. To this end, we employed solid-state NMR (ssNMR) to probe the structure and topology of isotopically labeled piscidins in the membrane-bound state.},
doi = {10.1021/ja058385e},
journal = {Journal of the American Chemical Society},
number = 16,
volume = 128,
place = {United States},
year = {Wed Apr 26 00:00:00 EDT 2006},
month = {Wed Apr 26 00:00:00 EDT 2006}
}