Combined effect of epigallocatechin gallate and triclosan on enoyl-ACP reductase of Mycobacterium tuberculosis

Among the various inhibitors known for enoyl-acyl carrier protein (ACP) reductases, triclosan and green tea catechins are two promising candidates. In the present study, we show, for the first time that epigallocatechin gallate (EGCG), a major component of green tea catechins, inhibits InhA, the eno...

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Bibliographic Details
Published in:	Biochemical and biophysical research communications Vol. 368; no. 1; pp. 12 - 17
Main Authors:	Sharma, Shailendra Kumar, Kumar, Gyanendra, Kapoor, Mili, Surolia, Avadhesha
Format:	Journal Article
Language:	English
Published:	United States Elsevier Inc 28-03-2008
Subjects:	Catechin - analogs & derivatives Catechin - chemistry Catechin - pharmacology EGCG Enoyl reductase Enoyl-(Acyl-Carrier-Protein) Reductase (NADH) - antagonists & inhibitors Enoyl-(Acyl-Carrier-Protein) Reductase (NADH) - chemistry Enoyl-(Acyl-Carrier-Protein) Reductase (NADH) - metabolism Enzyme Inhibitors - pharmacology Epigallocatechin gallate FAS I FAS II Fluorescence titration InhA Models, Molecular Molecular Structure Mycobacterium tuberculosis Mycobacterium tuberculosis - enzymology Protein Binding Protein Structure, Tertiary Scatchard plot Spectrometry, Fluorescence Tea catechins Triclosan Triclosan - chemistry Triclosan - pharmacology Tuberculosis Epigallocatechin gallate Tuberculosis Mycobacterium tuberculosis FAS II EGCG Enoyl reductase FAS I Tea catechins Scatchard plot Triclosan Fluorescence titration InhA
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Summary:	Among the various inhibitors known for enoyl-acyl carrier protein (ACP) reductases, triclosan and green tea catechins are two promising candidates. In the present study, we show, for the first time that epigallocatechin gallate (EGCG), a major component of green tea catechins, inhibits InhA, the enoyl-ACP reductase of Mycobacterium tuberculosis with an IC50 of 17.4μM. EGCG interferes with the binding of NADH to InhA. We also demonstrate that EGCG increased the inhibitory activity of triclosan towards InhA and vice versa. Direct binding assay using [3H]EGCG and fluorescence titration assay support the spectrophotometric/kinetic inhibition data. The biochemical data has been explained by docking simulation studies.
Bibliography:	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23
ISSN:	0006-291X 1090-2104
DOI:	10.1016/j.bbrc.2007.10.191