Please use this identifier to cite or link to this item: http://dspace.library.iitb.ac.in/xmlui/handle/100/13864
Title: Curcumin Recognizes a Unique Binding Site of Tubulin
Authors: CHAKRABORTI, S
DAS, L
KAPOOR, N
DAS, A
DWIVEDI, V
PODDAR, A
CHAKRABORTI, G
JANIK, M
BASU, G
PANDA, D
CHAKRABARTI, P
SUROLIA, A
BHATTACHARYYA, B
Keywords: Nf-Kappa-B
Mitochondrial Pathway
Apoptosis
Cells
Microtubules
Colchicine
Agents
Association
Inhibition
Activation
Issue Date: 2011
Publisher: AMER CHEMICAL SOC
Citation: JOURNAL OF MEDICINAL CHEMISTRY,54(18)6183-6196
Abstract: Although curcumin is known for its anticarcinogenic properties, the exact mechanism of its action or the identity of the target receptor is not completely understood. Studies on a series of curcumin analogues, synthesized to investigate their tubulin binding affinities and tubulin self-assembly inhibition, showed that: (i) curcumin acts as a bifunctional ligand, (ii) analogues with substitution at the diketone and acetylation of the terminal phenolic groups of curcumin are less effective, (iii) a benzylidiene derivative, compound 7, is more effective than curcumin in inhibiting tubulin self-assembly. Cell-based studies also showed compound 7 to be more effective than curcumin. Using fluorescence spectroscopy we show that curcumin binds tubulin 32 angstrom away from the colchicine-binding site. Docking studies also suggests that the curcumin-binding site to be close to the vinblastine-binding site. Structure-activity studies suggest that the tridented nature of compound 7 is responsible for its higher affinity for tubulin compared to curcumin.
URI: http://dx.doi.org/10.1021/jm2004046
http://dspace.library.iitb.ac.in/jspui/handle/100/13864
ISSN: 0022-2623
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