Modeling of Protein–Protein Interaction within Landau–Ginzburg–Wilson Approach Using α-Synuclein As an Example

Abstract

Parkinson’s disease is a neurodegenerative disease associated with the destruction of motor neurons. One of the biomarkers of the disease is Levy’s bodies, consisting mainly of α-synuclein protein. The protein forms aggregates, the mechanism of formation of which is still not fully understood. We propose a method for modeling protein–protein interaction by combining classical molecular dynamics methods and the Landau–Ginzburg–Wilson approach. The energy of the single protein chain is represented by the modernized Hamiltonian of the Abelian Higgs model. Interactions between different protein chains are taken into account due to the modernized Lennard–Jones potential and the Debye–Huckel potential. Two structures of α-synuclein were taken for the study: a micelle monomer and one of the tetramer molecules. Our results reveal that molecules derived from tetramers show a predisposition to form aggregates, while originally single molecules do not exhibit this tendency.