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Inhibition of lipoxygenase 1 by phosphatidylcholine micelles‐bound curcumin
Author(s) -
Began G.,
Sudharshan E.,
Rao A. G. Appu
Publication year - 1998
Publication title -
lipids
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.601
H-Index - 120
eISSN - 1558-9307
pISSN - 0024-4201
DOI - 10.1007/s11745-998-0327-2
Subject(s) - curcumin , micelle , chemistry , phosphatidylcholine , lipoxygenase , linoleic acid , curcuma , antioxidant , fatty acid , aqueous solution , stereochemistry , biochemistry , organic chemistry , nuclear chemistry , enzyme , phospholipid , biology , paleontology , membrane
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 μM 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 K l of 1.7 μM for linoleic and 4.3 μM 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.