Discovery and Characterization of a Disulfide-Locked C[subscript 2]-Symmetric Defensin Peptide
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Author(s)
Ziarek, Joshua J.
Wagner, Gerhard
Wommack, Andrew
Tomaras, Jill M
Chileveru, Haritha reddy
Zhang, Yunfei
Nolan, Elizabeth Marie
Date Issued
September 2014
Journal
Journal of the American Chemical Society
Publisher
American Chemical Society
Citation
Wommack, Andrew J., Joshua J. Ziare, Jill Tomaras, Haritha R.
Chileveru, Yunfei Zhang, Gerhard Wagner and Elizabeth M. Nolan. "Discovery and Characterization of a Disulfide-Locked C2-Symmetric Defensin Peptide." Journal of the American Chemical Society 136 (October 1 2014) (39): 13494–13497.
Version
Final published version
Abstract
We report the discovery of HD5-CD, an unprecedented C[subscript 2]-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[superscript II]–Cys[superscript IV] (Cys[superscript 5]–Cys[superscript 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.
MIT Department
Massachusetts Institute of Technology. Department of Chemistry
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DOI of Published Version
https://doi.org/10.1021/ja505957w
