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
USA
Email: bdunn@ufl.edu

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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.

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

Graphical Abstract:


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.

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Article Details

VOLUME: 22
ISSUE: 2
Page: [112 - 118]
Pages: 7
DOI: 10.2174/0929866521666140320104409