Abstract

Interaction of some cyclic chalcone analogs, (E)-2-(4-X-benzylidene)-1-benzosuberone derivatives with bovine serum albumin (BSA) and human serum albumin (HSA) has been investigated using UV-Vis spectroscopic methods. Recording the UV-Vis spectra of compounds in the presence of BSA or HSA indicated interaction of the molecules with the hydrophobic binding site(s) of the proteins. Investigated analogs have shown remarkable topo I and topo II inhibitory activity compared to camptothecin and etoposide, respectively, at 40 μM concentration. The observed interactions between the cyclic chalcone analogs and the cellular macromolecules might play a role in the previously detected cytotoxicity against several tumor cell lines.

Keywords

• cyclic chalcone analogs • enones • bovine serum albumin • human serum albumin • UV-Vis spectroscopy • DNA topoisomerases I and II