Sharif Digital Repository

Fluorescence spectroscopy in combination with circular dichroism (CD) spectroscopy were used to investigate the interaction of water-soluble amino acid Schiff base complexes, [Zn(L1,2)(phen)] where phen is 1,10-phenanthroline and H2L1,2 is amino acid Schiff base ligands, with bovine serum albumin (BSA) under the physiological conditions in phosphate buffer solution adjusted to pH 7.0. The quenching mechanism of fluorescence was suggested as static quenching according to the Stern-Volmer equation. Quenching constants were determined using the Stern-Volmer equation to provide a measure of the binding affinity between amino acid Schiff base complexes and BSA. The thermodynamic parameters ΔG, ΔH... 

Bio-inspired Human Serum Albumin (HSA) imprinted polydopamine nano-layer was produced through oxidative polymerization of dopamine on the pore surface of HSA modified porous silica particles. The coating thickness was controlled by the reaction time and thereby varied within 0-12. nm. The samples were characterized by elemental analysis, FT-IR, DSC, SEM, TEM, TGA, physisorption and thermoporometry. The characterization confirmed the success of evolution and deposition of polydopamine layer on the silica pore surface. Batch rebinding experiment showed that the molecularly imprinted polymer (MIP) with 8.7. nm coating thickness, in comparison with the thinner and thicker coatings, displays the... 

The cellular microenvironment can be engineered through the utilization of various nano-patterns and matrix-loaded bioactive molecules. In this study, a multilayer system of electrospun scaffold containing chitosan nanoparticles was introduced to overcome the common problems of instability and burst release of proteins from nanofibrous scaffolds. Bovine serum albumin (BSA)-loaded chitosan nanoparticles was fabricated based on ionic gelation interaction between chitosan and sodium tripolyphosphate. Suspension electrospinning was employed to fabricate poly-e{open}-caprolacton (PCL) containing protein-loaded chitosan nanoparticles with a core-shell structure. To obtain the desired scaffold... 

Circular dichroism (CD) spectroscopy, cyclic voltammetry (CV) and differential pulse voltammetry (DPV) were used to investigate the interaction between copper(II) complex of compartmental Schiff base ligand (L), N,N′-bis(3-hydroxysalicylidene)ethylenediamine, and bovine serum albumin (BSA) in 0.1 mol dm-3 phosphate buffer solution adjusted to physiological pH 7.0 containing 20% (w/w) dimethylsulfoxide at room temperature. CD spectra show that the interaction of the copper(II) complex with BSA leads to changes in the α-helical content of BSA and therefore changes in secondary structure of the protein with the slight red shift (2 nm) in CD spectra. From the voltammetric data, i.e. changes in...