Discovery and Characterization of a Disulfide-Locked C[subscript 2]-Symmetric Defensin Peptide

Discovery and Characterization of a Disulfide-Locked C[subscript 2]-Symmetric Defensin Peptide

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 I...

Full description

Bibliographic Details
Main Authors: Ziarek, Joshua J. (Author), Wagner, Gerhard (Author), Wommack, Andrew (Contributor), Tomaras, Jill M (Contributor), Chileveru, Haritha reddy (Contributor), Zhang, Yunfei (Contributor), Nolan, Elizabeth Marie (Contributor)
Other Authors: Massachusetts Institute of Technology. Department of Chemistry (Contributor)
Format: Article
Language:English
Published: American Chemical Society, 2017-05-16T15:26:43Z.
Subjects:
Article
Online Access:Get fulltext
Description
Summary: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.
United States. National Institutes of Health (DP2OD007045)
United States. National Institutes of Health (PO1 GM047467)
United States. National Institutes of Health (F32GM103005)
United States. National Institutes of Health (EB-002026)
National Science Foundation (U.S.) (Grant NSF-007031)

Similar Items