SCHIFF BASES AS POTENTIAL INHIBITORS OF AMINOPEPTIDASE N AS ANTICANCER AGENTS
| Authors | |
|---|---|
| Year of publication | 2022 |
| Type | Appeared in Conference without Proceedings |
| MU Faculty or unit | |
| Citation | |
| Description | Many Schiff bases appear to be important intermediates in a number of enzymatic reactions. The presence of the azomethine group, as well as their interesting physical and chemical properties, cause the widespread application of their metal complexes. Synthesized groups of basic thiosemicarbazone and semicarbazone derivatives of acetophenone have these properties as well. Aminopeptidase N (AP-N), or membrane alanyl aminopeptidase (m-AAP), is a neutral zinc-binding metallopeptidase that cleaves N-terminal residues from protein and peptides. This aminopeptidase turns out to be identical to the human cluster differentiation antigen CD13 expressed on the surface of myeloid progenitors and myeloid leukemia cells. |
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