Kaur, Simranjeet ; Modi, Niraj H. ; Panda, Dulal ; Roy, Nilanjan (2010) Probing the binding site of curcumin in Escherichia coli and Bacillus subtilis FtsZ- a structural insight to unveil antibacterial activity of curcumin European Journal of Medicinal Chemistry, 45 (9). pp. 4209-4214. ISSN 0223-5234
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Official URL: http://linkinghub.elsevier.com/retrieve/pii/S02235...
Related URL: http://dx.doi.org/10.1016/j.ejmech.2010.06.015
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 coli 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.
| Item Type: | Article |
|---|---|
| Source: | Copyright of this article belongs to Elsevier Science. |
| Keywords: | FtsZ; B. subtilis; Cytoskeleton Proteins; MEP; CD; Binding Analysis |
| ID Code: | 34937 |
| Deposited On: | 14 Apr 2011 13:56 |
| Last Modified: | 19 Apr 2011 09:29 |
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