화학공학소재연구정보센터
Journal of Physical Chemistry B, Vol.114, No.30, 9778-9786, 2010
Curcumin Disorders 1,2-Dipalmitoyl-sn-glycero-3-phosphocholine Membranes and Favors the Formation of Nonlamellar Structures by 1,2-Dielaidoyl-sn-glycero-3-phosphoethanolamine
Curcumin is a polyphenol present in turmeric, a spice widely used in Asian traditional medicine and cooking. It has many and diverse biological effects and is incorporated in cell membranes. This paper describes the mode in which curcumin modulates the physical properties of 1,2-dipalmitoyl-sn-glycero-3-phosphocholine (DPPC) and 1,2-dielaidyl-sn-glycero-3-phosphoetnanolamine (DEPE) multilamellar membranes. Curcumin disordered DPPC membranes at temperatures below T-c as seen by DSC, FT-IR, H-2 NMR, WAXD, and SAXD. The decrease induced by curcumin in T-c suggested that it is oriented in the bilayer with its main axis parallel to the acyl chains. Above T-c, too, curcumin introduced disorder as seen by infrared spectroscopy which showed that curcumin also alters the conformation of the polar group of DPPC, increasing the percentage of unhydrated C=O groups, but does not form hydrogen bonds with either the C=O group or the phosphate group of DPPC. Small angle X-ray diffraction showed a notable increase in the repeating spacings as a result of the presence of curcumin, suggesting the formation of a rippled phase. Increasing concentrations of curcumin progressively modified the onset and completion of the phase transition and also Delta H up to a 6:1 DPPC/curcumin molar ratio. A further increase of curcumin concentration did not produce effects on the transition parameters, suggesting that there is a limit for the solubility of curcumin in DPPC. Additionally, when DEPE was used to test the effect of curcumin on the phospholipid polymorphism, it was found that the temperature at which the H-II phase is formed decreased, indicating that curcumin favors negative curvature of the membrane, which may be important for explaining its effect on membrane dynamics and on membrane proteins or on proteins which may be activated through membrane insertion.