Probing the Interactions of Lamotrigine and Phenobarbital with Tau Protein: Experimental and Molecular Modeling Studies.

ABSTRACT: Tau, as a small protein in neurons, plays a main role in stabilizing and assembling the internal microtubules. Here, the effects of antiepileptic drugs, including lamotrigine (LTG) and phenobarbital (PHB), on tau protein structure have been investigated by surface plasmon resonance (SPR), fluorescence spectroscopy along molecular modeling. Fluorescence data analysis revealed that both drugs quench the intrinsic emission intensity of tau protein via a static quenching mechanism. Analysis of SPR data at three different temperatures revealed that binding of LTG and PHB to tau protein leads to a decrease and increase in equilibrium constants (K_D) values with increasing temperature, respectively. Therefore, the affinity of LTG decreases and PHB increases with increasing temperature.

SUBMITTER: Gholami A 

PROVIDER: S-EPMC10024808 | biostudies-literature | 2022 Dec

REPOSITORIES: biostudies-literature