The Schiff-base (PNOAAP) derived from picolinaldehyde N-oxide and 4-aminoantipyrine, and its copper(Ⅱ) complex: [Cu(PNOAAP)2(EtOH)2]2(ClO4)4 (1) has been prepared and characterized by elemental analysis, i.r., 1H n.m.r, spectrum, and single crystal X-ray crystallographic determination. The PNOAAP ligand isomerizes from trans to cis after chelating to copper(Ⅱ).

The binding equilibrium between I- and human serum albumin (HSA) or bovine serum albumin (BSA) has been studied by means of the resonance Rayleigh scattering (RRS) and equi librium dialysis. It has been found for the first time that RRS and multiple frequency scattering (MFS) are enhanced as the I- binding to the HSA and BSA, but fluorescence quenches. The equilibrium dialysis results suggest that the binding of I

The mechanisms and effects about the interaction between serum albumins and silver nanoparticles have been intensively studied by means of transmission electron microscopy (TEM), circular dichroism (CD) and ultraviolet-visible (UV-Vis) spectroscopy. The adsorption of serum albumins on the surface of silver nanoparticles is observed by TEM. The studies with the surface plasmon bands indicate that the electrostatic and hydrophilic interactions are the major forces between serum albumins and silver nanoparticles; the number of adsorbed monolayer serum albumin molecules to a silver nanoparticle with the size of 60nm is about 6.7

The binding equilibrium between phosphotungstic acid (H7[P(W2OT)6]

Synthesis and crystal structure determination of the title complex are presented. It shows that the zinc atom located in the distorted tetrahedral coordination, is composed of two nitrogen atoms and two sulfur atoms from the two ligand.

The interaction between Ag+ and human serum albumin (HSA) has been intensively studied by means of equilibrium dialysis, ligand-to-metal charge transition (LMCT) bands, circular dichroism (CD) and Raman spectroscopy. Scatchard analysis of the results of 1 equilibrium dialysis indicates the presence of two types of binding sites for Ag+ on HSA, and the orders of magnitude of binding stability 54 constants are found to be 10 5 and 10 4, respectively. During the binding process, a gradual increase in absorbance values of LMCT bands is observed with time-scanning UV absorption spectra, implying the Ag(Ⅰ) centers are continually formed in HSA. The time-scanning CD1 spectra provide evidence that the binding of Ag+ induces HSA to undergo a slow rearrangement of tertiary structure, and to change from 11 the original conformation in the absence of Ag (B-state) to conformation binding with Ag (A-state). The rate constants and activation free energy of A-B transition are calculated. The Raman spectrum of Ag(Ⅰ)-HSA system shows distinct vibration bands at 224 and 246 21cm in the low-frequency region, which significantly reveal the formation of Ag-S and Ag-N bonds. In addition, the electrostatic 1 interaction between Ag+ and negatively charged oxygen is also detected with Raman spectroscopy.

A notable hysteretic effect has been observed in the interaction of Co(Ⅱ) with human serum albumin (HSA) or bovine serum albumin (BSA) using UV-Visible spectrometry at physiological pH (7.43), which shows that the binding between Co(Ⅱ) and HSA or BSA may induce a slow transition of HSA or BSA from the conformation of weaker affinity for Co(Ⅱ) to one of stronger affinity (A-B transition). The rate constants and activation parameters of this transition were measured and are discussed. It is inferred that such a conformation transition may occur due to the binding of the first Co(Ⅱ) ion with the peptide segment of N-terminal residues 1-3, which results in a 'hinged movement' of the relatively hydrophobic 'valley' in the IA subdomain. This process leads to a slow conformational transition in the albumins, makes the other binding sites of Co(Ⅱ) exposed, and shows a positive cooperativity effect. The LMCT (ligand-to-metal charge transition) bands of the Co(Ⅱ)-HSA and Co(Ⅱ)-BSA systems also show a kind of hypochromic effect featuring a dipole-dipole interaction mechanism. This phenomenon is rarely reported.

The hydrothermal reaction of norfloxacin (H-Norf) with NH4VO3 yields an unprecedented neutral nanosized molecular square grid containing a direct coordinate bond between quinololine drug and V(Ⅱ), V(Norf)2·2H2O 1, which is characterized by single Xray determination and IR spectrum as well as TGA.

The aminosilane-modified magnetite nanoparticles were synthesized by the coprecipitation and surface modification with 3-aminopropyltriethoxysilane (APTTS). The superparamagnetic APTTS/Fe3O4 nanospheres with an average diameter of 10nm were characterized significantly with functional group, well dispersion and stabilization in aqueous fluids, as well as a maximized saturation magnetization of 63.54emu/g.

The reaction of picolinic acid (Hpic) and (n-Bu4N)4[MosO26] in the presence of CH3CN gave a supramolecular compound (n-Bu4N)2[Mo2O6(pic)2] (1), and its structure was characterized by elemental analysis, IR spectra and single crystal Xray diffraction analysis. The single crystal X-ray diffraction study shows that the crystal is in monocnnic crystal system, P21/c space group with cell parameters a=0.9941 (2), b=1.3719(2), c=1.8824(2)nm, β=100.840(10)°, Mr=508.50, V=2.5214(9)nm3, F(000)=1072. Compound 1 is a dimer through two μ2-O bridging to two MoO3 (pic)-unit, then connected one-dlmensional anion-chain by undassical hy-drogen bonding, and the anion-chain across the channels formed via (n-Bu4N)+ cations. By means of undassical hydrogen bonding, the anion-chain and cationchannels assemble into three-dimensional supramolecular networks.