Effect of Temperature and Solvent on Fibrillation of Human Serum Albumin
Nitin K. Pandey, Sudeshna Ghosh, Debi R. Tripathy and Swagata Dasgupta
Pages 112-118 (7)
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.
Ethanol, fibrillation, human serum albumin, solvent, spectroscopy, temperature.
Department of Chemistry, Indian Institute of Technology, Kharagpur, 721302, India.