Strong inhibitory effects of curcumin and its demethoxy analog on Escherichia coli ATP synthase F1 sector

Curcumin, a dietary phytopolyphenol isolated from a perennial herb (Curcuma longa), is a well-known compound effective for bacterial infections and tumors, and also as an antioxidant. In this study, we report the inhibitory effects of curcumin and its analogs on the Escherichia coli ATP synthase F1...

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Bibliographic Details
Published in:International journal of biological macromolecules 2014-09, Vol.70, p.241-245
Main Authors: Sekiya, Mizuki, Chiba, Eiko, Satoh, Momoe, Yamakoshi, Hiroyuki, Iwabuchi, Yoshiharu, Futai, Masamitsu, Nakanishi-Matsui, Mayumi
Format: Article
Language:English
Subjects:
ATP synthase
Bacterial Proton-Translocating ATPases - antagonists & inhibitors
Bacterial Proton-Translocating ATPases - chemistry
Bacterial Proton-Translocating ATPases - metabolism
Curcumin
Curcumin - analogs & derivatives
Curcumin - chemistry
Curcumin - pharmacology
Dose-Response Relationship, Drug
Enzyme Activation - drug effects
Escherichia coli - drug effects
Escherichia coli - enzymology
Escherichia coli - growth & development
F-ATPase
Oxidative Phosphorylation - drug effects
Structure-Activity Relationship
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Summary:Curcumin, a dietary phytopolyphenol isolated from a perennial herb (Curcuma longa), is a well-known compound effective for bacterial infections and tumors, and also as an antioxidant. In this study, we report the inhibitory effects of curcumin and its analogs on the Escherichia coli ATP synthase F1 sector. A structure–activity relationship study indicated the importance of 4′-hydroxy groups and a β-diketone moiety for the inhibition. The 3′-demethoxy analog (DMC) inhibited F1 more strongly than curcumin did. Furthermore, these compounds inhibited E. coli growth through oxidative phosphorylation, consistent with their effects on ATPase activity. These results suggest that the two compounds affected bacterial growth through inhibition of ATP synthase. Derivatives including bis(arylmethylidene)acetones (C5 curcuminoids) exhibited only weak activity toward ATPase and bacterial growth.
ISSN:0141-8130
1879-0003
DOI:10.1016/j.ijbiomac.2014.06.055