Protein & Peptide Letters

Prof. Ben M. Dunn  
Department of Biochemistry and Molecular Biology
University of Florida
College of Medicine
P.O. Box 100245
Gainesville, FL


Effect of Temperature and Solvent on Fibrillation of Human Serum Albumin

Author(s): Nitin K. Pandey, Sudeshna Ghosh, Debi R. Tripathy and Swagata Dasgupta

Affiliation: Department of Chemistry, Indian Institute of Technology, Kharagpur, 721302, India.

Graphical Abstract:


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.

Order Reprints Order Eprints Rights & PermissionsPrintExport

Article Details

Page: [112 - 118]
Pages: 7
DOI: 10.2174/0929866521666140320104409