RESUMO
A polymeric compound formulized as [Cu(µ-dipic)2{Na2(µ-H2O)4]n.2nH2O (I), where dipic is 2,6-pyridine dicarboxylic acid (dipicolinic acid, H2dipic), was synthesized by sonochemical irradiation. The initial in-vitro cytotoxic activity of this complex compared with renowned anticancer drugs like cisplatin, versus HCT116 colon cell lines, shows promising results. This study investigated the interaction mode between compound (I) and calf-thymus DNA utilizing a range of analytical techniques including spectrophotometry, fluorimetry, partition coefficient analysis, viscometry, gel electrophoresis and molecular docking technique. The results obtained from experimental methods reveal complex (I) could bind to CT-DNA via hydrogen bonding and van der Waals forces and the theoretical methods support it. Also, complex (I) indicates nuclease activity in the attendance of H2O2 and can act as an artificial nuclease to cleave DNA with high efficiency.Communicated by Ramaswamy H. Sarma.
RESUMO
A new Fe3O4@SiO2 fluorescent probe for detection of Hg2+ in aqueous solutions was introduced based on a simple ligand. The prepared sample was characterized by using TEM, EDX, FT-IR, VSM, and TGA/DTA. The sensitivity of the probe toward Hg2+ and its selectivity in presence of other cations were proven by using fluorescence spectroscopy. The detection limit of the prepared chemosensor is 8.1 nM. The magnetic property of the prepared nanocomposite enables its separation by an external magnet. The simple structure of the employed ligand results in simple preparation procedure and therefore could be an applicable material for detection of Hg2+ in industrial, environmental, and biological samples.
RESUMO
In this study, a cytotoxic Pt(IV) complex [Pt(5,5'-dmbpy)Cl4 (5,5'-dmbpy is 5,5'-dimethyl-2,2'-bipyridine) was selected to investigate its affinity to human serum albumin (HSA) by spectroscopy and molecular docking methods. This complex has a bidentate nitrogen donor ligand with four chloride anions attached to a Pt(IV) metal in a distorted octahedral environment. The ï¬uorescence data showed this complex quench the intrinsic ï¬uorescence of HSA through a static quenching mechanism. The binding constant (Kb) and the number of binding sites (n) were obtained based on the results of fluorescence measurements. UV-vis, circular dichroism spectroscopy, and three-dimensional fluorescence spectroscopy proved that the Pt(IV) complex could slightly change the secondary structure of protein. Thermodynamic parameters show that the Pt(IV) complex binds to HSA through electrostatic and Vander Waals interactions with one binding site. The molecular docking results confirmed the spectroscopic results and showed that Pt(IV) complex is embedded into subdomain IIA of protein. The aim of this study is to describe the performance of effective anti-cancer drugs when faced with proteins such as HSA.