| Summary: | The reaction of interaction of benzhydroxamic and 4-nitrobenzhydroxamic acids with succinyl chloride, carried out in an acetonitrile medium during boiling, was studied. It was revealed that the result of the reaction is the formation of <i>N</i>,<i>N</i>′-[succinylbis(oxy)]dibenzamides, the structure of which was proved by <sup>1</sup>H, <sup>13</sup>C NMR. Using the online program PASS, the biological activity of the obtained compounds was predicted. It was found that <i>N</i>,<i>N</i>′-[succinylbis(oxy)]dibenzamides can inhibit cathepsins (enzymes that degrade protein) with a high probability. Using the online program Mcule, the molecular docking of the obtained dibenzamides and their analogs with cathepsin S and cathepsin K was carried out, and ligands with the highest affinity for the cathepsin family were identified. Using the HyperChem program, semiempirical methods were used to analyze the possibility of synthesizing suitable ligands.
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