Specific Interaction With Human Serum Albumin Reduces Ginsenoside Cytotoxicity in Human Umbilical Vein Endothelial Cells.

ABSTRACT: Human serum albumin (HSA) is an important component of plasma, which has the functions of maintaining colloid osmotic pressure and capillary membrane stability, promoting blood circulation, and anti-oxidation. Three-dimensional structure of HSA determines its ability to bind and transport hormones and other substances. In this study we examined the interactions between HSA and ginsenoside Rg3, Rg5, Rk1, Rh2, and Rh4, which are the main cytotoxic ginsenosides extracted from red ginseng. Heat transfer generated by the specific interaction between HSA and each ginsenoside was measured using isothermal titration calorimetry (ITC) assay, which demonstrated that all these 5 ginsenosides bound to HSA with binding constants of 3.25, 1.89, 6.04, 2.07, and 5.17 × 105 M-1, respectively. Molecular doc

SUBMITTER: Li H 

PROVIDER: S-EPMC7201041 | biostudies-literature | 2020

REPOSITORIES: biostudies-literature