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

Vila Perello, Miguel; Sánchez Vallet, Andrea; García Olmedo, Francisco; Molina Fernández, Antonio y 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.

Descripción

Título: Structural dissection of a highly knotted peptide reveals minimal motif with antimicrobial activity
Autor/es:
  • Vila Perello, Miguel
  • Sánchez Vallet, Andrea
  • García Olmedo, Francisco
  • Molina Fernández, Antonio
  • Andreu, David
Tipo de Documento: Artículo
Título de Revista/Publicación: Journal of Biological Chemistry
Fecha: Enero 2005
Volumen: 280
Materias:
Escuela: E.T.S.I. Agrónomos (UPM) [antigua denominación]
Departamento: Biotecnologia [hasta 2014]
Licencias Creative Commons: Reconocimiento - Sin obra derivada - No comercial

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Resumen

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.

Más información

ID de Registro: 7624
Identificador DC: http://oa.upm.es/7624/
Identificador OAI: oai:oa.upm.es:7624
Identificador DOI: 10.1074/jbc.M410577200
URL Oficial: http://www.jbc.org/content/280/2/1661.full
Depositado por: Memoria Investigacion
Depositado el: 20 Jun 2011 08:57
Ultima Modificación: 18 Abr 2016 06:47
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