DSC study of SARS-CoV-2 ORF10 protein and its complexes with water-soluble metal phthalocyanines

Abstract

A theoretical and experimental study of the interaction of the SARS-CoV-2 ORF10 protein with sulfosubstituted cobalt(II) and copper(II) phthalocyanines was carried out. The structures of the most probable complexes of metal phthalocyanines with the ORF10 protein were obtained by molecular docking methods. Cobalt(II) tetrasulfophthal ocyanine binds to the protein in the monomeric state, while the interaction ofORF1 0 with copper(II) tetrasulfophthalocyanine causes aggregation of the formed protein complexes, which was shown by the UV-Vis spectroscopy. Thermal denaturation of the ORF10 protein and its complexes with metal phthalocyanines was studied by differential scanning calorimetry. A joint analysis of the spectral and thermochemical data made it possible to propose a description of the mechanism of thermal denaturation ofthe ORF10 protein.