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

IR@IMTECH: CSIR-Institute of Microbial Technology, Chandigarh


Field	Value

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