Interaction of nitrobenzoxadiazole derivatives of piperazine and aniline with bovine serum albumine in silico and in vitro

Albumin is a globular protein of plasma of mammalian blood participating in transport of hydrophobic metabolites and drugs. Thus, studies devoted to its binding are valuable as a part of evaluation of new potential drugs or fluorescent probes for in vivo usage. Here we describe results concerning synthesis and bovine serum albumin binding assay both in silico (docking) and in vitro (spectrophotometric and spectrofluorimetric titrations) for four new 7-nitrobenzoxadiazol-4-yl (NBD) derivatives of aniline and piperazine. Experimental dissociation constant for NBD-ethynylaniline 4 was calculated to be about 10 µmol/L.

Synthesis of a conductive polymer thin film having a choline phosphate side group and its bioadhesive properties

A conductive polymer thin film having choline phosphate as the side group was prepared. The polymer thin film can prevent bovine serum albumin binding while present nice fibroblast cell adhesion.

Synthesis, crystal structure and bovine serum albumin–binding studies of a new Cd(II) complex incorporating 2,2′-(propane-1,3-diyl)bis(1H-imidazole-4,5-dicarboxylate)

A new Cd(II) complex, [Cd(H4pbidc)(H2O)] n (1), incorporating 2,2′-(propane-1,3-diyl)bis(1H- imidazole-4,5-dicarboxylic acid) (H6pbidc) was synthesized and characterized by elemental analysis, infrared spectra and X-ray single-crystal diffraction. In complex 1, each Cd(II) ion is hepta-coordinated, showing a significantly distorted pentagonal-bipyramidal coordination environment. Adjacent Cd(II) ions are alternately joined through two carboxylate oxygen atoms and two bridging water molecules resulting in a one-dimensional chain structure. In the solid state, adjacent chains are further linked by hydrogen bonds, forming a three-dimensional supramolecular architecture. Meanwhile, the interactions of complex 1 with bovine serum albumin were analysed by fluorescence measurements under physiological conditions. The results indicated that the fluorescence intensity of bovine serum albumin was decreased considerably upon the addition of complex 1 through a static quenching mechanism with formation of one binding site. The negative values of the thermodynamic parameters including enthalpy change (Δ H), entropy change (Δ S) and Gibbs free energy change (Δ G) showed that hydrogen bonding and van der Waals forces were the main interactions in the binding of complex 1 to bovine serum albumin, and the binding process is spontaneous in thermodynamics.