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Probing the binding site of curcumin in Escherichia coli and Bacillus subtilis FtsZ - A structural insight to unveil antibacterial activity of curcumin

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Title Probing the binding site of curcumin in Escherichia coli and Bacillus subtilis FtsZ - A structural insight to unveil antibacterial activity of curcumin
 
Creator KAUR, S
MODI, NH
PANDA, D
ROY, N
 
Subject bacterial-cell-division
flexible docking
scoring function
protein ftsz
tubulin
ring
antibiotics
inhibitors
algorithm
discovery
ftsz
b. subtilis
cytoskeleton proteins
mep
cd
binding analysis
 
Description 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. .
 
Publisher ELSEVIER FRANCE-EDITIONS SCIENTIFIQUES MEDICALES ELSEVIER
 
Date 2011-07-21T17:07:11Z
2011-12-26T12:52:06Z
2011-12-27T05:39:06Z
2011-07-21T17:07:11Z
2011-12-26T12:52:06Z
2011-12-27T05:39:06Z
2010
 
Type Article
 
Identifier EUROPEAN JOURNAL OF MEDICINAL CHEMISTRY, 45(9), 4209-4214
0223-5234
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
 
Language en