Structural dissection of a highly knotted peptide reveals minimal motif with antimicrobial activity

Vila Perello, Miguel and Sánchez Vallet, Andrea and García Olmedo, Francisco and Molina Fernández, Antonio and Andreu, David (2005). Structural dissection of a highly knotted peptide reveals minimal motif with antimicrobial activity. "Journal of Biological Chemistry", v. 280 (n. 2); pp. 1661-1668. ISSN 0021-9258. https://doi.org/10.1074/jbc.M410577200.

Description

Title: Structural dissection of a highly knotted peptide reveals minimal motif with antimicrobial activity
Author/s:
  • Vila Perello, Miguel
  • Sánchez Vallet, Andrea
  • García Olmedo, Francisco
  • Molina Fernández, Antonio
  • Andreu, David
Item Type: Article
Título de Revista/Publicación: Journal of Biological Chemistry
Date: January 2005
ISSN: 0021-9258
Volume: 280
Subjects:
Faculty: E.T.S.I. Agrónomos (UPM) [antigua denominación]
Department: Biotecnologia [hasta 2014]
Creative Commons Licenses: Recognition - No derivative works - Non commercial

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Abstract

The increasing occurrence of bacterial resistance to antibiotics is driving a renewed interest on antimicrobial peptides, in the hope that understanding the structural features responsible for their activity will provide leads into new anti-infective drug candidates. Most chemical studies in this field have focused on linear peptides of various eukaryotic origins, rather than on structures with complex folding patterns found also in nature. We have undertaken the structural dissection of a highly knotted, cysteine-rich plant thionin, with the aim of defining a minimal, synthetically accessible, structure that preserves the bioactive properties of the parent peptide. Using efficient strategies for directed disulfide bond formation, we have prepared a substantially simplified (45% size reduction) version with undiminished antimicrobial activity against a representative panel of pathogens. Analysis by circular dichroism shows that the downsized peptide preserves the central double alpha-helix of the parent form as an essential bioactive motif. Membrane permeability and surface plasmon resonance studies confirm that the mechanism of action remains unchanged.

More information

Item ID: 7624
DC Identifier: http://oa.upm.es/7624/
OAI Identifier: oai:oa.upm.es:7624
DOI: 10.1074/jbc.M410577200
Official URL: http://www.jbc.org/content/280/2/1661.full
Deposited by: Memoria Investigacion
Deposited on: 20 Jun 2011 08:57
Last Modified: 18 Apr 2016 06:47
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