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

Journal Article · Wed Apr 26 04:00:00 EDT 2006 · Journal of the American Chemical Society

DOI:https://doi.org/10.1021/ja058385e· OSTI ID:889058

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

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.

• Research Organization: Pacific Northwest National Laboratory (PNNL), Richland, WA (US), Environmental Molecular Sciences Laboratory (EMSL)
• Sponsoring Organization: USDOE
• DOE Contract Number: AC05-76RL01830
• OSTI ID: 889058
• Journal Information: Journal of the American Chemical Society, Journal Name: Journal of the American Chemical Society Journal Issue: 16 Vol. 128; ISSN JACSAT; ISSN 0002-7863
• Country of Publication: United States
• Language: English

Related Subjects

59 BASIC BIOLOGICAL SCIENCES
Environmental Molecular Sciences Laboratory
FISHES
MAST CELLS
MEMBRANES
MORPHOLOGY
NUCLEAR MAGNETIC RESONANCE
PEPTIDES
STRUCTURE-ACTIVITY RELATIONSHIPS
TOPOLOGY