Fibrillation of human serum albumin shows nonspecific coordination on stoichiometric increment of Copper(II)

摘要: Protein aggregation is related to a series of pathological disorders the main cause which are fibrillar species generated during process. Human serum albumin (HSA) undergoes rapid fibrillation in presence Cu(II) at pH 7.4 60% ethanol after 6-h incubation (∼65 °C) followed by room temperature incubation. Here, we have investigated effect stoichiometric variation on self-assembly HSA using Congo red and thioflavin T dye-binding studies, circular dichroism spectroscopy, Fourier transform infrared electron paramagnetic resonance fluorescence microscopy transmission microscopy. The simulation EPR spectra suggests that with increment ion concentration, there change ligand field coordination. Kinetic parameters indicate reduced cooperativity may be nonspecific coordination concentration. also able direct accumulation large number fibers along formation dense network evident from microscopic images.