Synthetic and structural studies on Pyrularia pubera thionin: a single-residue mutation enhances activity against Gram-negative bacteria

Vila Perello, Miguel and Sánchez Vallet, Andrea and García Olmedo, Francisco and Molina Fernández, Antonio and Andreu, David (2003). Synthetic and structural studies on Pyrularia pubera thionin: a single-residue mutation enhances activity against Gram-negative bacteria. "Febs Letters", v. 536 (n. 1-3); pp. 215-219. ISSN 0014-5793. https://doi.org/10.1016/S0014-5793(03)00053-X.

Description

Title: Synthetic and structural studies on Pyrularia pubera thionin: a single-residue mutation enhances activity against Gram-negative bacteria
Author/s:
  • Vila Perello, Miguel
  • Sánchez Vallet, Andrea
  • García Olmedo, Francisco
  • Molina Fernández, Antonio
  • Andreu, David
Item Type: Article
Título de Revista/Publicación: Febs Letters
Date: February 2003
ISSN: 0014-5793
Volume: 536
Subjects:
Freetext Keywords: Thionin; Antimicrobial peptide; Oxidative folding; Plant
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 thionin from Pyrularia pubera (Pp-TH), a 47-residue peptide with four internal disulfide bonds, was efficiently produced by chemical synthesis. Its antimicrobial activity in vitro against several representative pathogens (EC50=0.3–3.0 μM) was identical to that of natural Pp-TH. This peptide has a unique Asp32 instead of the consensus Arg found in other thionins of the same family. In order to evaluate the effect of this mutation, the Arg32 analogue (Pp-TH(D32R)) was also synthesized and showed a significant increase in antibiotic activity against several Gram-negative bacteria, whereas it retained the same activity against other pathogens. The overall structure of Pp-TH(D32R) was maintained, though a slight decrease in the helical content of the peptide was observed.

More information

Item ID: 5805
DC Identifier: http://oa.upm.es/5805/
OAI Identifier: oai:oa.upm.es:5805
DOI: 10.1016/S0014-5793(03)00053-X
Official URL: http://www.sciencedirect.com/science/article/pii/S001457930300053X
Deposited by: Memoria Investigacion
Deposited on: 26 Jan 2011 11:01
Last Modified: 20 Apr 2016 14:31
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