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Purification, biochemical characterization and self-assembled structure of a fengycin-like antifungal peptide from Bacillus thuringiensis strain SM1.

DIR@IMTECH: CSIR-Institute of Microbial Technology

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Title Purification, biochemical characterization and self-assembled structure of a fengycin-like antifungal peptide from Bacillus thuringiensis strain SM1.
 
Creator Roy, Anupam
Mahata, Denial
Paul, Debarati
Korpole, Suresh
Franco, Octavio L
Mandal, Santi M
 
Subject QR Microbiology
 
Description An antifungal lipopeptide fengycin, producing strain SM1 was isolated from farm land soil sample and identified as Bacillus thuringiensis strain SM1 by using 16S rDNA analysis. Fengycin detected in the culture extract was further purified using HPLC and showed a molecular mass of 1492.8 Da by MALDI-TOF-MS analysis. Purified fengycin was allowed to construct their self-assembled structure onto a hydrophobic surface showing a clear improvement of antibacterial activity. In self-assembly, fengycin adapts a spherical micelle core shell like structure. Self-assembled fengycin may be a successful antimicrobial compound modifying its action from confined antifungal function. Besides it can open up a new area of research in supramolecular lipopeptide based compound making. This can revealed the mode of action of this unique self-assembled structure to fully evaluate its potential for use as an antimicrobial drug to control the emergence of bacterial infection.
 
Publisher Frontiers Media
 
Date 2013
 
Type Article
PeerReviewed
 
Relation https://doi.org/10.3389/fmicb.2013.00332
http://crdd.osdd.net/open/2453/
 
Identifier Roy, Anupam and Mahata, Denial and Paul, Debarati and Korpole, Suresh and Franco, Octavio L and Mandal, Santi M (2013) Purification, biochemical characterization and self-assembled structure of a fengycin-like antifungal peptide from Bacillus thuringiensis strain SM1. Frontiers in microbiology, 4. p. 332. ISSN 1664-302X