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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 constants was detected with the increase of temperatures (298-308 K) and the binding constants were in range from 1.32 × 105 to 4.3 × 103 L mol-1 indicating the instability of the BSA and rivaroxaban complex at higher temperatures. The data of number of binding sites showed uniformity. The site marker experiments indicated site I (sub-domain IIA) as the principal site for rivaroxaban binding. The thermodynamic study experiments were carried at the temperatures of 298/303/308 K. The ?G0, ?H0 and ?S0 at these temperatures ranged between - 24.67 and - 21.27 kJ mol-1 and the values for ?H0 and ?S0 were found to be - 126 kJ mol-1 and ?S - 340 J mol-1 K-1 The negative value of ?G0 indicating spontaneous binding between the two molecules. The negative values in ?H0 and ?S0 indicated van der Waals interaction and hydrogen bonding were involved during the interaction between rivaroxaban and BSA. CONCLUSIONS:The results of molecular docking were consistent with the results obtained from spectroscopic studies in establishing the principal binding site and type of bonds between rivaroxaban and BSA.

SUBMITTER: Wani TA

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

REPOSITORIES: biostudies-literature

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

Wani Tanveer A TA AlRabiah Haitham H Bakheit Ahmed H AH Kalam Mohd Abul MA Zargar Seema S

Chemistry Central journal 20171220 1

<h4>Background</h4>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 ...[more]

PMID: 29260434

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Project description:BackgroundBovine serum albumin (BSA) contains high affinity binding sites for several endogenous and exogenous compounds and has been used to replace human serum albumin (HSA), as these two compounds share a similar structure. Naringin palmitate is a modified product of naringin that is produced by an acylation reaction with palmitic acid, which is considered to be an effective substance for enhancing naringin lipophilicity. In this study, the interaction of naringin palmitate with BSA was characterised by spectroscopic and molecular docking techniques.Methodology/principal findingsThe goal of this study was to investigate the interactions between naringin palmitate and BSA under physiological conditions, and differences in naringin and naringin palmitate affinities for BSA were further compared and analysed. The formation of naringin palmitate-BSA was revealed by fluorescence quenching, and the Stern-Volmer quenching constant (KSV ) was found to decrease with increasing temperature, suggesting that a static quenching mechanism was involved. The changes in enthalpy (?H) and entropy (?S) for the interaction were detected at -4.11 ± 0.18 kJ·mol(-1) and -76.59 ± 0.32 J·mol(-1)·K(-1), respectively, which indicated that the naringin palmitate-BSA interaction occurred mainly through van der Waals forces and hydrogen bond formation. The negative free energy change (?G) values of naringin palmitate at different temperatures suggested a spontaneous interaction. Circular dichroism studies revealed that the ?-helical content of BSA decreased after interacting with naringin palmitate. Displacement studies suggested that naringin palmitate was partially bound to site I (subdomain IIA) of the BSA, which was also substantiated by the molecular docking studies.Conclusions/significanceIn conclusion, naringin palmitate was transported by BSA and was easily removed afterwards. As a consequence, an extension of naringin applications for use in food, cosmetic and medicinal preparations may be clinically and practically significant, especially in the design of new naringin palmitate-inspired drugs.

Dataset Information

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

Publications

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

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