Effect of temperature and solvent on fibrillation of human serum albumin

During the past several years,studies on the protein aggregation process in the presence of cosolvents/co-solutes have been looked into which provides significant insight in the stability of proteins in a crowded cellular milieu. here,in the present report we have investigated the fibrillation of human serum albumin (hsa) under the mixed aqueous-ethanol solvent conditions at two different temperatures (37 °c and 65 °c). self-association of protein was monitored using various spectroscopic and microscopic techniques. results obtained from detailed investigation have shown that fibrillation of human serum albumin is favored at higher temperature (65 °c) at lower ethanol concentration. however,at 37 °c comparatively higher ethanol concentration is the prerequisite condition for fibrillation process to take place. © 2015 bentham science publishers.