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2hfr
From Proteopedia
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solution structure of antimicrobial peptide Fowlicidin 3
Overview
Cathelicidins are an important family of cationic host defense peptides in, vertebrates with both antimicrobial and immunomodulatory activities., Fowlicidin-1 and fowlicidin-2 are two newly identified chicken, cathelicidins with potent antibacterial activities. Here we report, structural and functional characterization of the putatively mature form, of the third chicken cathelicidin, fowlicidin-3, for exploration of its, therapeutic potential. NMR spectroscopy revealed that fowlicidin-3, comprises 27 amino-acid residues and adopts a predominantly alpha-helical, structure extending from residue 9 to 25 with a slight kink induced by a, glycine at position 17. It is highly potent against a broad range of, Gram-negative and Gram-positive bacteria in vitro, including, antibiotic-resistant strains, with minimum inhibitory concentrations in, the range 1-2 microM. It kills bacteria quickly, permeabilizing, cytoplasmic membranes immediately on coming into contact with them. Unlike, many other host defense peptides with antimicrobial activities that are, diminished by serum or salt, fowlicidin-3 retains bacteria-killing, activities in the presence of 50% serum or physiological concentrations of, salt. Furthermore, it is capable of suppressing lipopolysaccharide-induced, expression of proinflammatory genes in mouse macrophage RAW264.7 cells, with nearly complete blockage at 10 microM. Fowlicidin-3 appears to be an, excellent candidate for future development as a novel antimicrobial and, antisepsis agent, particularly against antibiotic-resistant pathogens.
About this Structure
2HFR is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.
Reference
Fowlicidin-3 is an alpha-helical cationic host defense peptide with potent antibacterial and lipopolysaccharide-neutralizing activities., Bommineni YR, Dai H, Gong YX, Soulages JL, Fernando SC, Desilva U, Prakash O, Zhang G, FEBS J. 2007 Jan;274(2):418-28. PMID:17229147
Page seeded by OCA on Tue Jan 29 20:20:18 2008
