SCHIFF BASES AS POTENTIAL INHIBITORS OF AMINOPEPTIDASE N AS ANTICANCER AGENTS

Varování

Publikace nespadá pod Fakultu sportovních studií, ale pod Farmaceutickou fakultu. Oficiální stránka publikace je na webu muni.cz.

Autoři	BALLAYOVÁ Veronika ŽÁČKOVÁ Radka KAUEROVÁ Tereza KOLLÁR Peter FARSA Oldřich
Rok publikování	2022
Druh	Další prezentace na konferencích
Fakulta / Pracoviště MU	Farmaceutická fakulta
Citace
Popis	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.
Související projekty:	Basic ketones and their derivatives as potential anti-infective and anti-tumor drugs