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 × 10 L mol. 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.

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) (H O) ], 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) (H O) ] complex and the quenching mechanism was considered as static quenching by formation of a [Cu(carmoisine) (H O) ]-HSA complex. The binding constant was about 10  M at room temperature.

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

The interaction of a new macrocyclic copper complex, [CuL(NO)] in which L is 1,3,6,10,12,15-hexaaza tricyclo[13.3.1.

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.

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.