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.
Keywords: Ethanol, fibrillation, human serum albumin, solvent, spectroscopy, temperature.
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