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J Am Chem Soc. 2014 Oct 1;136(39):13494-7. doi: 10.1021/ja505957w. Epub 2014 Sep 23.

Discovery and characterization of a disulfide-locked C(2)-symmetric defensin peptide.

Author information

1
Department of Chemistry, Massachusetts Institute of Technology , Cambridge, Massachusetts 02139, United States.

Abstract

We report the discovery of HD5-CD, an unprecedented C2-symmetric β-barrel-like covalent dimer of the cysteine-rich host-defense peptide human defensin 5 (HD5). Dimerization results from intermonomer disulfide exchange between the canonical α-defensin Cys(II)-Cys(IV) (Cys(5)-Cys(20)) bonds located at the hydrophobic interface. This disulfide-locked dimeric assembly provides a new element of structural diversity for cysteine-rich peptides as well as increased protease resistance, broad-spectrum antimicrobial activity, and enhanced potency against the opportunistic human pathogen Acinetobacter baumannii.

PMID:
25181039
PMCID:
PMC4183617
DOI:
10.1021/ja505957w
[Indexed for MEDLINE]
Free PMC Article

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