Complexation of curcumin with cyclodextrins adjusts its binding to plasma proteins
Yao Hu, Chaojun Guo, Qianzhu Lin, Jiali Hu, Xiaojing Li, Shangyuan Sang, David Julian McClements, Jie Long, Zhengyu Jin, Jinpeng Wang, Chao Qiu
Abstract
and from 0.80 to 1.15 in the absence and presence of SACD, respectively. The presence of SACD also reduced the ability of curcumin to promote conformational changes in BSA. For instance, the thermal denaturation temperatures of BSA in BSA-curcumin mixtures was 65.3 °C and 67.0 °C in the absence and presence of SACD, respectively, compared to 67.8 °C for pure BSA. These effects were attributed to the fact that SACD forms an inclusion complex with curcumin and modulates the binding of curcumin with BSA, which may affect the biological accessibility of curcumin in the systemic circulation.
Topics & Concepts
CurcuminChemistrySolubilityAqueous solutionSystemic circulationPlasma concentrationPlasma protein bindingBlood proteinsPlasmaCombinatorial chemistryChromatographyBiochemistryPharmacologyOrganic chemistryBiologyInternal medicineMedicinePhysicsQuantum mechanicsCurcumin's Biomedical ApplicationsProtein Interaction Studies and Fluorescence AnalysisProteins in Food Systems