Analysis of the binding mechanism for a water-soluble Pd(II) complex containing ß-amino alcohols with HSA applying experimental and computational methods.

In the study ahead, the binding interactions of the [Pd (HEAC) Cl2] complex with human serum albumin (HSA) protein have been assayed in vitro (pH= 7.40) utilizing computational and experimental procedures. The mentioned complex was synthesized as a water-soluble complex from {2-((2-((2-hydroxyethyl)amino)ethyl)amino) cyclohexanol} ligand = HEAC. The results of electronic absorption and circular dichroism investigations illustrated that the hydrophobicity of the Tryptophan microenvironment in HSA undergoes the changes by binding to the Pd(II) complex without substantial perturbations on the protein secondary structure. The fluorescence emission spectroscopy analysis revealed that with rising temperature, the quenching constant (Ksv) in the Stern-Volmer's relation decreases; so, it can be said that the interaction process is along with a static quenching mechanism. The values of 2.88 × 105 M-1, and 1.26 represent the binding constant (Kb) and the number of the binding sites (n), respectively. The Job graph showed the maximum point at χ = 0.5, which means organizing a new set with 1:1 stoichiometry. Thermodynamic profile (ΔH < 0, ΔS < 0, and ΔG < 0) has affirmed that van der Waals forces and hydrogen bonds have a basic function in the Pd(II) complex-albumin bindings. The ligand-competitive displacement studies utilizing warfarin and ibuprofen have represented that Pd(II) complex interacts with albumin by site II (subdomain IIIA). The computational molecular docking theory approved the results of the site-competitive tests; also, it indicated the existence of hydrogen bonds and van der Waals forces in Pd(II) complex-albumin interactions.Communicated by Ramaswamy H. Sarma.

Interaction studies of water-soluble Zn(II) complex with calf thymus DNA using biophysical and molecular docking methods".

The binding between a fluorescent water-soluble Zn(II) complex of {2-[N-(2-hydroxyethylammonioethyl) imino methyl] phenol} and calf thymus DNA (ct-DNA) was investigated using spectroscopic techniques. The complex was prepared and identified by FT-IR, and 1H NMR spectroscopies. The significant changes in the absorption and the circular dichroism spectra of ct-DNA in the presence of the Zn(II) complex implied the interaction between the Zn(II) complex and ct-DNA. Upon addition of ct-DNA, the fluorescence emission intensity of the Zn(II) complex was increased and indicated the interaction between the Zn(II) complex and ct-DNA was occurred. The binding constant values (Kb) resulted from fluorescence spectra clearly showed the Zn(II) complex affinity to ct-DNA. The fluorescence studies also approved the static enhancement mechanism in the Zn(II) complex-DNA complexation process. The thermodynamic profile exhibited the exothermic and spontaneous formation of ct-DNA-Zn(II) complex system via hydrogen bonds and van der Waals forces. The competitive fluorescence investigation by methylene blue (MB), and Hoechst 33258 demonstrated that the Zn(II) complex could replace the DNA-bound Hoechst and bind to the minor groove binding site in ct-DNA. The viscosity changes were negligible, representing the Zn(II) complex binding to DNA via the groove binding mode. Molecular docking simulation affirmed that the Zn(II) complex is located in the minor groove of ct-DNA near the DG12, DA17, DA18, and DG16 nucleobases.

Successful simultaneous retrieval of two dislodged and entangled intracoronary stents using distal balloon inflating technique.

Stent loss in coronary arteries is a rare complication of coronary intervention. Furthermore, the entanglement of a lost stent with a second previously deployed stent leading to a very complicated scenario has not been reported previously. In this case, we are presenting the first case report of a stent loss due to the entanglement of a stent with the ostial part of the second already deployed side branch stent leading to distortions of the second stent and entrapment. This is also the first case report describing the successful and simultaneous retrieval of both the lost and entangled deployed stents percutaneously using the distal inflating balloon technique.

Experimental and Molecular Docking Studies on the Interaction of a Water-Soluble Pd(II) Complex Containing ß-Amino Alcohol with Calf Thymus DNA.

The interaction of water-soluble and fluorescent [Pd (HEAC) Cl2] complex, in which HEAC is 2-((2-((2-hydroxyethyl)amino)ethyl)amino) cyclohexanol, with calf thymus DNA (ct-DNA) has been studied. This study was performed using electronic absorption and fluorescence emission spectroscopies, cyclic voltammetry and circular dichroism analyses, dynamic viscosity measurements, and molecular docking theory. From hypochromic effect observed in ct-DNA absorption spectra, it was found that the Pd(II) complex could form a conjugate with ct-DNA strands through the groove binding mode. The Kb values obtained from fluorescence measurements clearly assert the Pd(II) complex affinity to ct-DNA. The fluorescence quenching of the DNA-Hoechst compound following the successive additions of the Pd(II) complex to the solution revealed that the Pd(II) complex is located in the ct-DNA grooves, and Hoechst molecules have been released into solution; moreover, the resulting measurements from relative viscosity authenticate the Pd(II) complex binding to the grooves. Negative quantities of thermodynamic parameters imply that the Pd(II) complex binds to ct-DNA mainly by the hydrogen bonds and van der Waals forces; also, the Gibbs-free energy changes show the exothermic and spontaneous formation of the Pd(II) complex-DNA system. The electrochemical behavior of the Pd(II) complex in the attendance of ct-DNA was investigated using the cyclic voltammetry method (CV). Several quasi-reversible redox waves were observed along with increasing the anodic/cathodic peak currents, as well as a shift in anodic/cathodic peak potentials. Circular dichroism (CD) observations suggested that the Pd(II)-DNA interaction could alter ct-DNA conformation. The results of molecular modeling confirmed that groove mechanism is followed by the Pd(II) complex to interact with ct-DNA.