Which priority area of science and technology corresponds to: fundamental scientific research on the most important problems of developing scientific, technical, socio-economic, socio-political, human potential to ensure the competitiveness of Ukraine in the world and the sustainable development of society and the state;
Research: purely fundamental.
Future application perspective: completed study
Research level: no analogues in Ukraine.
Availability of a patent: 1 patent.
What additional actions require further research: additional funding, modern scientific equipment.
Brief description, advantages, further perspective.
For the screening of tyrosinase inhibitors (EC 1.14.18.1), an enzyme with a 25% increased activity was isolated from Agaricusbisporus fungi using a modified method. A search for new tyrosinase inhibitors was carried out among a wide range of compounds, including derivatives of 3-chloro-1,4-naphthoquinone, isatin, 3-hydroxy-2-pephthoic acid, etc. 50 benzylideneaniline derivatives and related compounds were synthesized with yields of 48.5-98% close to those given in the literature. It was shown that the studied substances are effective inhibitors of tyrosinase, IC5016 of which is 1.5-7.7 times less than such a standard tyrosinase inhibitor – kojic acid. It was found that the replacement of the hydroxyl groups of the benzylideneaniline molecule with a carboxy-, methoxy-, nitro-, sulfo group, the use of cyclohexylamine, 4-aminoantipyrine, 3-amino-1,2,4-triazole, 2-glucosamine and 6-aminopenicilan. for the synthesis of Schiff bases, leads to a sharp decrease in the inhibition of the enzyme by the studied compounds. It has been established that the studied benzylideneaniline derivatives are non-competitive tyrosinase inhibitors: the inhibition constant varies from 5.1 to 115.0 µmol/dm3 depending on the structure of the compound.
Based on tyrosinase immobilized in poly-N-vinylpyrrolidone, a multiple-acting biocatalyst promising for the synthesis of L-DOPA (L-3,4-dihydroxyphenylalanine, drugs for the treatment of Parkinson’s disease) has been created. It was determined that in methylene chloride containing 2% Na-phosphate buffer solution (pH 6.5), the activity of immobilized tyrosinase exceeded that of free tyrosinase by 30%. The immobilized enzyme catalyzes the oxidation of the substrate with 80% conversion and maintaining a high degree of conversion for 6 cycles of use.