Journal
PEPTIDES
Volume 24, Issue 11, Pages 1795-1805Publisher
ELSEVIER SCIENCE INC
DOI: 10.1016/j.peptides.2003.08.020
Keywords
innate immunity; paneth cells; polymerase chain reaction; recombinant peptide expression; alpha-defensin; reverse-phase high performance liquid; chromatography; matrix-assisted laser desorption time-of-flight mass spectrometry; surface plasmon resonance; lipid polydiacetylene vesicles; ANTS-DPX leakage; antimicrobial peptide
Funding
- NIAID NIH HHS [AI22931] Funding Source: Medline
- NIDDK NIH HHS [DK44632, DK10184] Funding Source: Medline
- NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES [R01AI022931, R37AI022931] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES [R01DK044632, F32DK010184, R55DK044632] Funding Source: NIH RePORTER
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Paneth cells secrete alpha-defensins into the lumen from the base of small intestinal crypts, and cryptdin-4 (Crp4) is the most potent mouse alpha-defensin in vitro. Purified recombinant Crp4 and Crp4 variants with (des-Gly)-, (Gly1Val)-, (G1y1Asp)-, and (Gly1Arg)-substitutions were all bactericidal with Crp4 and (Gly1Arg)-Crp4 being slightly more active than other variants. Bactericidal activities correlated directly with permeabilization of live Escherichia coli, with equilibrium binding to E. coli membrane phospholipid bilayers and vesicles, and with induced graded fluorophore leakage from phospholipid vesicles. The Crp4 peptide N-terminus affects bactericidal activity modestly, apparently by influencing peptide binding to phospholipid bilayers and subsequent permeabilization of target cell membranes. (C) 2003 Elsevier Inc. All rights reserved.
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