Interaction studies of copper complex containing food additive carmoisine dye with human serum albumin (HSA): Spectroscopic investigations.

In this study, the interaction between human serum albumin (HSA) and a copper complex of carmoisine dye; [Cu(carmoisine)2 (H2 O)2 ], was studied in vitro using multi-spectroscopic methods. It was found that the intrinsic fluorescence of HSA was quenched by the addition of the [Cu(carmoisine)2 (H2 O)2 ] complex and the quenching mechanism was considered as static quenching by formation of a [Cu(carmoisine)2 (H2 O)2 ]-HSA complex. The binding constant was about 104  M-1 at room temperature. The values of the calculated thermodynamic parameters (ΔH < 0 and ΔS > 0) suggested that both hydrogen bonds and the hydrophobic interactions were involved in the binding process. The site marker competitive experiments revealed that the binding of [Cu(carmoisine)2 (H2 O)2 ] to HSA primarily occurred in subdomain IIIA (site II) of HSA. The results of circular dichroism (CD) and UV-vis spectroscopy showed that the micro-environment of amino acid residues and the conformation of HSA were changed after addition of the [Cu(carmoisine)2 (H2 O)2 ] complex. Finally, the binding of the [Cu(carmoisine)2 (H2 O)2 ] complex to HSA was modelled by a molecular docking method. Excellent agreement was obtained between the experimental and theoretical results with respect to the binding forces and binding constant.

Molecular docking and spectroscopic studies on the interaction of new fifth-generation antibacterial drug ceftobiprole with calf thymus DNA.

The interaction of the cefobiprole drug with calf thymus DNA (ct-DNA) at physiological pH was investigated by UV-visible spectrophotometry, fluorescence measurement, dynamic viscosity measurements, circular dichroism spectroscopy and molecular modeling. The binding constant obtained of UV-visible was 4 × 104 L mol-1. Moreover, the results of circular dichroism (CD) and viscosity measurements displayed that the binding of the cefobiprole to ct-DNA can change the conformation of ct-DNA. Furthermore, thermodynamic parameters indicated that hydrogen bond and van der waals play main roles in the binding of cefobiprole to ct-DNA. Optimal results of docking, it can be concluded that ceftobiprole-DNA docked model is in approximate correlation with our experimental results.

Experimental and molecular modeling studies on the DNA-binding of diazacyclam-based acrocyclic copper complex.

The interaction of a new macrocyclic copper complex, [CuL(NO3)2] in which L is 1,3,6,10,12,15-hexaaza tricyclo[13.3.1.16,10] eicosane was investigated in vitro under simulated physiological conditions by multi-spectroscopic techniques and molecular modeling study. The fluorescence spectroscopy and UV absorption spectroscopy indicated the complex interacted with ct-DNA in a groove binding mode while the binding constant of UV-vis and the number of binding sites were 1.0±0.2×104Lmol-1 and 1.01, respectively. The fluorometric studies showed that the reaction between the complex with ct-DNA is exothermic (ΔH=14.85kJmol-1; ΔS=109.54Jmol-1K-1). Circular dichroism spectroscopy (CD) was employed to measure the conformational change of DNA in the presence of [CuL(NO3)2] complex. Furthermore, the complex induces detectable changes in the viscosity of DNA. The molecular modeling results illustrated that the complex strongly binds to groove of DNA. Experimental and molecular modeling results showed that Cu(II) complex bound to DNA by a groove binding mode.

Molecular modeling and multispectroscopic studies of the interaction of mesalamine with bovine serum albumin.

The interaction of mesalamine (5-aminosalicylic acid (5-ASA)) with bovine serum albumin (BSA) was investigated by fluorescence quenching, absorption spectroscopy, circular dichroism (CD) techniques, and molecular docking. Thermodynamic parameters (ΔH<0 and ΔS 0) indicated that the hydrogen bond and electrostatic forces played the major role in the binding of 5-ASA to BSA. The results of CD and UV-vis spectroscopy showed that the binding of this drug to BSA induces some conformational changes in BSA. Displacement experiments predicted that the binding of 5-ASA to BSA is located within domain III, Sudlows site 2, that these observations were substantiated by molecular docking studies. In addition, the docking result shows that the 5-ASA in its anionic form mainly interacts with Gln-416 residue through one hydrogen bond between H atom of 5-ASA anion and the adjacent O atom of the hydroxyl group of Gln-416.

Study on the interaction of the drug mesalamine with calf thymus DNA using molecular docking and spectroscopic techniques.

The interaction of CT-DNA with the drug mesalamine (5-ASA) at physiological pH has been investigated by absorption, emission, circular dichroism (CD), cyclic voltammetry (CV), viscosity studies and molecular modeling. Thermodynamic parameters (ΔH>0 and ΔS<0) indicated that hydrogen bond and van der Waals play main roles in the binding of 5-ASA to CT-DNA. Ethidium bromide (EB) displacement studies revealed that 5-ASA did not have any effect on ethidium bromide (EB) bound DNA which is indicative of groove binding. The results obtained from experimental and molecular modeling showed that 5-ASA is a minor groove binder of DNA and preferentially binds to GC rich regions.