Investigation of Interaction of Some Chalcones and Cyclic Chalcone Analogues with Outer Mitochondrial Membrane by UV-VIS and Fluorescence Spectroscopy

Abstract

Interaction of the synthetic chalcones (1b,1c) and their cyclic analogues (2b,2c) with bovine (BSA) and human serum albumin (HSA) as well as with rat liver mitochondria (RLM) was studied by fluorescence spectroscopy. The maxima of emission fluorescence spectra were changed only in the case of 2b and 2c during interaction with BSA, HSA as well as mitochondrial outer membrane showing a slight hypsochromic shift and decrease of fluorescence. Interaction of the methoxy-(1b,2b) and the dimethylamino-substituted (1c,2c) compounds with outer mitochondrial membrane were studied by fluorescence polarization. Fluorescence polarization of 1b in the presence of the two proteins and mitochondria was found to be unchanged. Under similar conditions (2b,1c,2c) showed continuously increasing fluorescence polarization signal during the 30 minute period of investigations. Since fluorescence polarization supposes that as a result of binding these substances to proteins and lipids. Compound 2c displayed a continuous increase of fluorescence polarization signal in the presence of proteins (BSA, HSA), yeast cytoplasm (YC) and mitochondria (YM and RLM). This compound displayed a significant cytotoxic effect. This pattern of interaction with proteins might be one of the contributing vectors of the observed cytotoxicity against several human carcinoma cell lines.

Luminescence, circular dichroism and in silico studies of binding interaction of synthesized naphthylchalcone derivatives with bovine serum albumin

“…The blue shift suggested that the Trp residue is buried in the hydrophobic environment of the BSA protein, which signifies that binding of the ligands creates a more apolar environment around the Trp residue . Some previous studies have reported the binding of chalcones with serum proteins, but most have reported a blue shift in the wavelength maxima in the fluorescence emission spectra of the serum protein . The shift in the wavelength maxima of BSA in the presence of naphthylchalcone derivatives suggests their binding to BSA.…”

“…[23][24][25] Some previous studies have reported the binding of chalcones with serum proteins, but most have reported a blue shift in the wavelength maxima in the fluorescence emission spectra of the serum protein. [26,27] The shift in the wavelength maxima of BSA in the presence of naphthylchalcone derivatives suggests their binding to BSA.…”

Study on the interaction of some (E)-2-benzylidenebenzosuberone derivatives with serum albumin by UV-Vis method, inhibitory effect on topoisomerase

“…Such a remarkable effect of B2 on the G 1 and G 2 checkpoints could not be observed [14] . While investigating the mechanism of cytotoxicity of the compounds, the effect on the mitochondrial outer membrane of some (E)-2-arylmethylene-1-benzosuberone analogs was tested by fluorescence spectroscopy [16,17] . The effect of some analogs on isolated rat liver mitochondrial functions were also investigated.…”