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Information × Registration Number 0221U106617, 0120U100111 , R & D reports Title Search for new photocontrolled inhibitors of therapeutically important enzymes. popup.stage_title Head Kobzar Oleksandr L., к.х.н. Registration Date 16-12-2021 Organization V.P. Kukhar Institute of Bioorganic Chemistry and Petrochemistry of the National Academy of Sciences of Ukraine popup.description2  The photocontrolled properties of alkyl- and aryl-α-ketophosphonates, as well as the calix[4]arene α-ketophosphonіc acids as inhibitors of glutathione S-transferases were studied for the first time. Alkyl- and aryl-α-ketophosphonates, which demonstrated photo-dependent inhibition activities on these enzymes with IC50 values in the micromolar range, did not show such effects on activities of protein tyrosine phosphatases and alkaline phosphatases, as well as leucine aminopeptidase and xanthine oxidase. The photocontrolled inhibition of cholinesterases by alkyl- and aryl-α-ketophosphonates was lower compared to the inhibition of glutathione S-transferases. The ability of alkyl- and aryl-α-ketophosphonates to quench the intrinsic fluorescence of bovine serum albumin under UV irradiation, which may be associated with the modification of its amino acid residues, has also been showed. For the first time, the approach of using a calix[4]arene scaffold for designing derivatives bearing α-ketophosphonate fragment as photocontrolled inhibitors of glutathione S-transferases and protein tyrosine phosphatases was substantiated. It was found that photoactivated inactivation of the enzymes in the presence calix[4]arenes α-ketophosphonic acids depends on the nature of the substituents on the lower rim as well as the number and modification of α-ketophosphonate groups on the upper rim of the macrocyclic platform. Herewith the photoactivated inhibition of alkaline phosphatases, leucine aminopeptidase and xanthine oxidase by these compounds was weak. The photocontrolled inhibition of butyrylcholinesterase by calix[4]arene α-ketophosphonic acids was selective over acetylcholinesterase. Product Description popup.authors Buldenko Vladyslav M. Mrug Galyna P. Shulga Yuriy V. popup.nrat_date 2021-12-16 Close