Myeline basic protein (MBP) is the second most abundant protein present in the central nervous system. MBP maintains the correct structure of Myeline, a lipid-rich substance that surrounds nerve cell axons like a sheath. The myeline sheath primarily works as an insulator that promotes efficient transmission of electrical signal. Study suggests that alterations of MBP and isomers contribute to the early course of different demyelination diseases such as multiple sclerosis [1]. Direct or environmental exposure to different volatile and aromatic compounds can introduce these changes in the central nervous system. In this study, we have analyzed the association of MBP to highly volatile n-alkylbenzenes (benzene, toluene, ethylbenzene, n-propylbenzene, and n-butylbenzene) since these compounds are prevalent in gasoline, paints, cosmetics, plastics, insecticides, cleaning products, and inks. We employed a protein-ligand webserver, SwissDock [2], to predict the most possible binding free energies of MBP and these compounds. The binding free energies were compared with that of the experimental values measured by Equilibrium Headspace Gas Chromatography (EHSGC). The theoretical model showed the best possible locations of the compounds on MBP affected by the length of the alkyl sidechain. The experimental binding free energies show a clear trend with alkyl sidechain whereas the theoretical values do not, but they are of the same order of magnitude, -40 to -55 kJ/mol.

Association of myeline basic protein with n-alkylbenzenes: A computational docking experiment

ACS Spring Meeting 2021

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