Effect of temperature and solvent on fibrillation of human serum albumin.
Protein Pept Lett
; 22(2): 112-8, 2015.
Article
en En
| MEDLINE
| ID: mdl-24654852
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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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Albúmina Sérica
/
Agua
/
Etanol
Límite:
Humans
Idioma:
En
Revista:
Protein Pept Lett
Asunto de la revista:
BIOQUIMICA
Año:
2015
Tipo del documento:
Article