Please use this identifier to cite or link to this item: http://dspace.library.iitb.ac.in/xmlui/handle/10054/5931
Title: Probing the binding site of curcumin in Escherichia coli and Bacillus subtilis FtsZ - A structural insight to unveil antibacterial activity of curcumin
Authors: KAUR, S
MODI, NH
PANDA, D
ROY, N
Keywords: Bacterial-Cell-Division
Flexible Docking
Scoring Function
Protein Ftsz
Tubulin
Ring
Antibiotics
Inhibitors
Algorithm
Discovery
Issue Date: 2010
Publisher: ELSEVIER FRANCE-EDITIONS SCIENTIFIQUES MEDICALES ELSEVIER
Citation: EUROPEAN JOURNAL OF MEDICINAL CHEMISTRY, 45(9), 4209-4214
Abstract: The cytoskeletal protein, FtsZ plays a pivotal role in prokaryotic cell division and is present in majority of the bacterial species. In recent years, inhibitors of FtsZ have been identified that may function as lead compounds for the development of novel antimicrobials. It has been found that curcumin, the main bioactive component of Curcuma longa, inhibits Bacillus subtilis and Escherichia coil growth by inhibiting FtsZ assembly. Though it is experimentally established that curcumin inhibits FtsZ polymerization, the binding site of curcumin in FtsZ is not known. In this study, interaction of curcumin with catalytic core domain of E. coli and B. subtilis FtsZ was investigated using computational docking. (C) 2010 Elsevier Masson SAS. .
URI: http://dx.doi.org/10.1016/j.ejmech.2010.06.015
http://dspace.library.iitb.ac.in/xmlui/handle/10054/5931
http://hdl.handle.net/10054/5931
ISSN: 0223-5234
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