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Discovery and Characterization of a Disulfide-Locked C2‑Symmetric Defensin Peptide

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journal contribution
posted on 17.12.2015, 04:52 by Andrew J. Wommack, Joshua J. Ziarek, Jill Tomaras, Haritha R. Chileveru, Yunfei Zhang, Gerhard Wagner, Elizabeth M. Nolan
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 CysII–CysIV (Cys5–Cys20) 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.

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