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...
| Main Authors: | , , , , , , |
|---|---|
| Other Authors: | |
| Format: | Article |
| Language: | en_US |
| Published: |
American Chemical Society
2017
|
| Online Access: | http://hdl.handle.net/1721.1/109106 https://orcid.org/0000-0002-2515-5901 https://orcid.org/0000-0002-6426-2291 https://orcid.org/0000-0002-6153-8803 |
| 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. |
|---|