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

Andrew J. Wommack | Zendy; Joshua J. Ziarek | Zendy; Jill Tomaras | Zendy; Haritha R. Chileveru | Zendy; Yunfei Zhang | Zendy; Gerhard Wagner | Zendy; Elizabeth M. Nolan | Zendy

AI Assistant Blog Pricing

Home ZAIA Blog

Open Access

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

Author(s) -

Andrew J. Wommack,

Joshua J. Ziarek,

Jill Tomaras,

Haritha R. Chileveru,

Yunfei Zhang,

Gerhard Wagner,

Elizabeth M. Nolan

Publication year - 2014

Publication title -

journal of the american chemical society

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 7.115

H-Index - 612

eISSN - 1520-5126

pISSN - 0002-7863

DOI - 10.1021/ja505957w

Subject(s) - chemistry , defensin , cysteine , peptide , dimer , covalent bond , stereochemistry , peptide sequence , disulfide bond , biochemistry , enzyme , organic chemistry , gene

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.

The content you want is available to Zendy users.

Already have an account? Click here to sign in.

Having issues? You can contact us here

Accelerating Research