- PII
- 10.31857/S0132344X23600042-1
- DOI
- 10.31857/S0132344X23600042
- Publication type
- Status
- Published
- Authors
- Volume/ Edition
- Volume 49 / Issue number 10
- Pages
- 659-664
- Abstract
- The interaction of cobalt(II) tetrasulfophthalocyanine (CoPc) with the ORF8 accessory protein of SARS-CoV-2 was studied by spectroscopy and calorimetry. The protein was found to shift the aggregation equilibrium in cobalt tetrasulfophthalocyanine solutions towards dimerization. Most probably, the CoPc dimer binds to ORF8 on the greater β-sheet side, thus causing fluorescence quenching. The protein affinity constant to CoPc dimer is 1.5 × 105. Differential scanning calorimetry data indicate that ORF8 undergoes thermally induced denaturation in the temperature range of 38–67°C. Melting of ORF8 includes two stages, which partly overlap. The complex formation of ORF8 with CoPc leads to thermal stabilization of the protein, thus preventing the second stage of protein unfolding. Denaturation of the complex proceeds between 40 and 77°C as two temperature-separated stages. According to gel electrophoresis and immunoblotting data, visible light photoirradiation of the ORF8 complex with CoPc does not induce photooxidation of the protein. It was shown that water-soluble cobalt sulfo-substituted phthalocyanine can be considered as a potential drug inhibiting the ORF8 accessory protein.
- Keywords
- SARS-CoV-2 металлофталоцианины белок комплекс фотоинактивация
- Date of publication
- 01.10.2023
- Year of publication
- 2023
- Number of purchasers
- 0
- Views
- 10
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