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 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 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

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.