echinacoside and salvianolic-acid-B

The aim of the work was to determine the interactions of a set of anti-cancer compounds with bovine serum albumin (BSA) using a ProteOn XPR36 array biosensor and molecular docking studies. The results revealed that a total of six anti-cancer compounds: gallic acid, doxorubicin, acteoside, salvianolic acid B, echinacoside, and vincristine were able to reversibly bind to the immobilized BSA. The sensorgrams of these six compounds were globally fit to a Langmuir 1:1 interaction model for binding kinetics analysis. There were significant differences in their affinity for BSA, with doxorubicin, the weakest binding compound having 1000-fold less affinity than salvianolic acid B, the strongest binding compound. However, compounds with a similar KD often exhibited markedly different kinetics due to the differences in

Topics: Animals; Antineoplastic Agents; Benzofurans; Binding Sites; Biosensing Techniques; Cattle; Doxorubicin; Gallic Acid; Glucosides; Glycosides; Molecular Docking Simulation; Phenols; Protein Array Analysis; Protein Binding; Serum Albumin, Bovine; Surface Plasmon Resonance; Vincristine