Abstract Title:

Inhibition of lipoxygenase 1 by phosphatidylcholine micelles-bound curcumin.

Abstract Source:

Lipids. 1998 Dec;33(12):1223-8. PMID: 9930409

Abstract Author(s):

G Began, E Sudharshan, A G Appu Rao

Article Affiliation:

Department of Protein Chemistry and Technology, Central Food Technological Research Institute, Mysore, India.


Curcumin (diferuloyl methane) from rhizomes of Curcuma longa L. binds to phosphatidylcholine (PC) micelles. The binding of curcumin with PC micelles was followed by fluorescence measurements. Curcumin emits at 490 nm with an excitation wavelength of 451 nm after binding to PC-mixed micelles stabilized with deoxycholate. Curcumin in aqueous solution does not inhibit dioxygenation of fatty acids by Lipoxygenase 1 (LOX1). But, when bound to PC micelles, it inhibits the oxidation of fatty acids. The present study has shown that 8.6 microM of curcumin bound to the PC micelles is required for 50% inhibition of linoleic acid peroxidation. Lineweaver-Burk plot analysis has indicated that curcumin is a competitive inhibitor of LOX1 with Ki of 1.7 microM for linoleic and 4.3 microM for arachidonic acids, respectively. Based on spectroscopic measurements, we conclude that the inhibition of LOX1 activity by curcumin can be due to binding to active center iron and curcumin after binding to the PC micelles acts as an inhibitor of LOX1.

Study Type : In Vitro Study

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