Spectroscopic and molecular modeling studies of binding interaction between bovine serum albumin and roflumilast.

ABSTRACT:

Background

The binding interaction between bovine serum albumin (BSA) and roflumilast (ROF) was explored in this study. The binding of drugs to albumin plays a vital role in their pharmacokinetics and pharmacodynamics in vivo. The mechanisms involved in the interaction between BSA and ROF was studied using multi-spectroscopic experimental and computational approaches.

Materials and methods

Spectrofluorometric experiments were used to determine the method of quenching involved and the conformational changes in the BSA. UV-visible spectroscopy synchronous and three-dimensional fluorescence spectroscopy were used to further explore the binding interaction mechanism.

Results

The results suggested that the intrinsic fluorescence of BSA was quenched due to the formation of

SUBMITTER: Wani TA 

PROVIDER: S-EPMC6118266 | biostudies-literature | 2018

REPOSITORIES: biostudies-literature