A synthetic analog of plantaricin 149 inhibiting food-borne pathogenic bacteria:evidence for α-helical conformation involved in bacteria–membrane interaction
✍ Scribed by Diana M. Müller; Marta S. Carrasco; Arturo C. Simonetta; Leila M. Beltramini; Georgina G. Tonarelli
- Book ID
- 105360651
- Publisher
- John Wiley and Sons
- Year
- 2007
- Tongue
- English
- Weight
- 232 KB
- Volume
- 13
- Category
- Article
- ISSN
- 1075-2617
- DOI
- 10.1002/psc.828
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✦ Synopsis
Abstract
Plantaricin‐149 is a bacteriocin produced by Lactobacillus plantarum NRIC 149 (a LAB isolated from pineapple), which consists of a peptidic chain made up of 22 amino acid residues [Kato et al. J. Ferment. Bioeng. 1994; 77: 277–282]. In this work, a synthetic C‐terminal amidated peptide analog denoted Pln149a was prepared by SPPS‐Fmoc chemistry and the antagonistic activity against gram‐positive and gram‐negative bacteria was tested. The secondary structure was studied by circular dichroism (CD) and the vicinity of the tyrosine residue by fluorescence spectroscopy under different conditions. We report the results of the interaction of Pln149a with reverse micelles prepared from the amphiphilic AOT in cyclohexane.
Synthetic plantaricin was active against one strain of Staphylococcus aureus and four strains of Listeria genus at pH 5.5 and 7.4 and, like its natural variant, inhibited L. plantarum ATCC 8014.
The data derived from spectroscopic measurements in presence of AOT reverse micelles suggest that the secondary structure of the peptide upon interaction is an α‐helix. In this membrane model, the hydrophobic side of the α‐helix is inserted into the micelles, leaving the lysines exposed to the solvent and interacting with the polar moieties of AOT. The fluorescence data point out that the N‐terminal tyrosine residue is close to the micellar interface. Copyright © 2007 European Peptide Society and John Wiley & Sons, Ltd.