DNA damaging, cell cytotoxicity and serum albumin binding efficacy of the rutin–Cu(ii) complex. Issue 5 (1st April 2016)

• Record Type: Journal Article
• Authors: Roy, Atanu Singha; Tripathy, Debi Ranjan; Samanta, Sintu; Ghosh, Sudip K.; Dasgupta, Swagata
• Is Part Of: Molecular bioSystems. Volume 12:Issue 5(2016:May)
• Page Start: 1687
• Page End: 1701
• Publication Date: 2016-04-01
• Subjects: Molecular biology -- Periodicals; Biochemistry -- Periodicals; 571.7405
• DOI: 10.1039/c6mb00161k
• Languages: English
• ISSNs: 1742-206X

Abstract

Abstract : The rutin–Cu(ii ) complex causes DNA damage and is also able to inhibit the growth of human HeLa cells. This complex binds with serum albumins via hydrophobic forces. Abstract : Flavonoids are widely used as anti-oxidants, anti-cancer agents and possess metal ion chelation properties. In this report we have investigated the DNA binding (and damaging), cell cytotoxicity and serum albumin (SA) binding efficacy of the rutin–Cu(ii ) complex using differential spectroscopic methods. The rutin–Cu(ii ) complex was able to intercalate into calf thymus DNA (ct-DNA) at lower concentrations and its DNA damaging properties were also confirmed from the agarose gel based assay, fluorescence and UV-vis studies. The copper complex was found to be effective against the growth of HeLa cells in vivo . The binding constants ( K b ) of the rutin–Cu(ii ) complex towards HSA and BSA were found to be (0.98 ± 0.03) and (1.05 ± 0.02) × 10 5 M −1, respectively, at 299 K and observed to increase with the increase in temperature. Site selectivity studies revealed that the rutin–Cu(ii ) complex binds near site 1 (subdomain IIA) of SAs. Thermodynamic parameters indicated that the mode of interaction of rutin and its copper complex with SAs are different from each other. Both Δ H ° and Δ S ° were observed to be positive for the interaction of the rutin–Cu(ii ) complex with SAs, indicating the presence of hydrophobic association in binding. The values of Δ H ° were estimated to be negative (−42.07 ± 2.92 and −23.29 ± 2.33 kJ mol −1 for HSA and BSA respectively) in the binding of rutin with SAs. It implies that after chelation with Cu(ii ) ion, rutin alters its binding mode which could have varying applications to its other physicochemical activities.