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Article

Mechanisms of alpha-defensin bactericidal action: comparative membrane disruption by Cryptdin-4 and its disulfide-null analogue.

Biochemistry - 25 Nov 2008

Hadjicharalambous Chrystalleni, Sheynis Tania, Jelinek Raz, Shanahan Michael T, Ouellette Andre J, Gizeli Electra

Abstract excerpt

Mammalian alpha-defensins all have a conserved triple-stranded beta-sheet structure that is constrained by an invariant tridisulfide array, and the peptides exert bactericidal effects by permeabilizing the target cell envelope. Curiously, the disordered, disulfide-null variant of mouse alpha-defensin cryptdin-4 (Crp4), termed (6C/A)-Crp4, has bactericidal activity equal to or greater than that of the native...

Topics

Animals
Cell Membrane
Disulfides
Escherichia coli
Liposomes
Mice
Mutant Proteins
Mutation
Permeability
Phospholipids
Protein Structure, Secondary

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Protein Transport

alpha-Defensins

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Identifiers

PMID: 18973303
DOI: 10.1021/bi800335e
PMCID: PMC2645939

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