Inhibition of lipoxygenase 1 by phosphatidylcholine micelles-bound curcumin

• Published in: Lipids Vol. 33; no. 12; pp. 1223 - n/a
• Main Authors: Began, G. (Central Food Technology Research Institute, Mysore, India.), Sudharshan, E, Rao, A.G.A
• Format: Journal Article
• Language: English
• Published: Berlin/Heidelberg Springer‐Verlag 01.12.1998; Springer Nature B.V
• Subjects: Aquatic plants; Aqueous solutions; Arachidonic Acids - metabolism; Catalysis; Curcumin - chemistry; Curcumin - pharmacology; Fatty acids; INHIBICION; INHIBITION; LECITHINE; LECITHINS; LECITINAS; Linoleic Acid - metabolism; LIPOXIGENASA; LIPOXYGENASE; Lipoxygenase - drug effects; Lipoxygenase - metabolism; Lipoxygenase Inhibitors - chemistry; Lipoxygenase Inhibitors - pharmacology; Micelles; Microscopy, Fluorescence; NATURAL ANTIOXIDANTS; Oxidation-Reduction; Peroxidation; Phosphatidylcholines - chemistry
• DOI: 10.1007/s11745-998-0327-2
• ISSN: 0024-4201

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 Kl 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.