Exploring the interaction between 1,4-butanediol and acid phosphatase using spectroscopic techniques and molecular modeling studies

Abstract

The functional characteristics of enzymes greatly rely on their stability, which is a vital factor to be considered when utilizing these biomolecules in industrial settings. This study investigated the effects of 1,4-butanediol (BD) on the structure and activity of acid phosphatase (AP). To this end, an array of analytical techniques, such as circular dichroism (CD), thermal stability analysis, kinetic studies, fluorescence spectroscopy, molecular docking, and molecular dynamics (MD) simulations, were employed to elucidate the impact of BD on AP. The data gathered indicated that BD has a positive effect on enhancing the stability of AP. BD demonstrated its capability to bind to AP, leading to the quenching of AP's inherent fluorescence through the static quenching mechanism. The binding process was spontaneous, with van der Waals forces and hydrogen bonding serving as the primary interactions between BD and AP. The formation of the complex was also validated via UV–Vis. According to CD studies, the presence of BD induced alternations in the structure of AP. Further, docking studies showed the favored binding site of BD within the structure of AP. Besides, the kinetic parameters showed that BD could act as an activator for AP.