title: Effect of temperature and solvent on fibrillation of human serum albumin.
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.
authors.forename: Nitin K
authors.initials: NK
authors.lastname: Pandey
authors.forename: Sudeshna
authors.initials: S
authors.lastname: Ghosh
authors.forename: Debi R
authors.initials: DR
authors.lastname: Tripathy
authors.affiliation: Department of Chemistry, Indian Institute of Technology, Kharagpur, 721302, India. swagata@chem.iitkgp.ernet.in.
authors.forename: Swagata
authors.initials: S
authors.lastname: Dasgupta
mesh_terms: D052160:Benzothiazoles; D002942:Circular Dichroism; D000431:Ethanol / Q000737:chemistry*; D005454:Fluorescence Polarization; D006801:Humans; D046529:Microscopy, Electron, Transmission; D008856:Microscopy, Fluorescence; D011487:Protein Conformation; D055503:Protein Multimerization; D012709:Serum Albumin / Q000737:chemistry* / Q000378:metabolism*; D013696:Temperature; D013816:Thermodynamics; D013844:Thiazoles / Q000378:metabolism; D014867:Water / Q000737:chemistry*
chemical_list: D052160:Benzothiazoles; D012709:Serum Albumin; D013844:Thiazoles; D014867:Water; C009462:thioflavin T; D000431:Ethanol