Study of binding interaction of rivaroxaban with bovine serum albumin using multi-spectroscopic and molecular docking approach.

ABSTRACT: BACKGROUND:Rivaroxaban is a direct inhibitor of coagulation factor Xa and is used for venous thromboembolic disorders. The rivaroxaban interaction with BSA was studied to understand its PK and PD (pharmacokinetics and pharmacokinetics) properties. Multi-spectroscopic studies were used to study the interaction which included UV spectrophotometric, spectrofluorometric and three dimensional spectrofluorometric studies. Further elucidation of data was done by molecular simulation studies to evaluate the interaction behavior between BSA and rivaroxaban. RESULTS:Rivaroxaban quenched the basic fluorescence of BSA molecule by the process of static quenching since rivaroxaban and BSA form a complex that results in shift of the absorption spectra of BSA molecule. A decline in the values of binding c

SUBMITTER: Wani TA 

PROVIDER: S-EPMC5736510 | biostudies-literature | 2017 Dec

REPOSITORIES: biostudies-literature