Molecular docking and multi-spectroscopic approaches to unravel the mechanism of the interaction between thiocolchicoside and bovine serum albumin

Abstract

A popular muscle relaxant for the treatment of severe, painful muscular spasms is thiocolchicoside (TCS). Although the precise mechanism underlying its ability to relax muscles is unknown, it demonstrates a specific affinity for the inhibitory gamma-aminobutyric acid and glycinergic receptors. This study used a variety of spectroscopic methods and molecular docking to examine the interaction of TCS with bovine serum albumin (BSA). UV absorption and fluorescence spectroscopic titration analysis supported the conclusion that TCS suppressed BSA's fluorescence through a blend of static and dynamic mechanisms. The thermodynamical constraints revealed that the interaction between BSA and TCS is spontaneous and that van der Waals and hydrogen bonding forces play key roles in stabilising the complex. TCS binds to the site III on BSA, as demonstrated by competitive binding assays utilising site-specific markers and molecular docking studies. By binding TCS, BSA exhibits minor microenvironmental modifications near the tryptophan amino acid residue, according to a structural study employing synchronous fluorescent.