Differential stabilizing effects of buffers on structural stability of Bovine Serum Albumin against urea denaturation
Document Type
Article
Publication Date
1-1-2022
Abstract
The conformational stability of Bovine Serum Albumin (BSA) against urea denaturation was investigated in aqueous solutions both in the absence and presence of buffers. Various buffers differing in polar and nonpolar characters such as sodium phosphate, Tris-HCl, (4-(2-hydroxyethyl)-1-piperazineethanesulfonic acid) HEPES and 3-(N-morpholino)propanesulfonic acid] MOPS buffers were used in this study. Urea-induced structural changes were analyzed using different spectroscopic techniques, i.e., intrinsic fluorescence, ANS fluorescence and UV-difference spectroscopy. The presence of different buffers in the incubation medium offered different degrees of resistance to the protein against urea-induced structural changes. A similar trend of buffer-induced structural resistance was noticed with three different techniques. The stabilizing effect of these buffers followed the order: MOPS > HEPES > sodium phosphate > Tris-HCl > pure water. The highest stability of BSA observed in MOPS, and HEPES buffers can be attributed to the presence of morpholine and piperazine rings in their structures, respectively. These groups might have produced a hydrophobic environment around the protein surface, stabilizing protein conformation against urea denaturation.
Keywords
Bovine serum albumin, HEPES, MOPS, Protein stability, Urea denaturation
Divisions
Science
Publication Title
Latin American Applied Research
Volume
52
Issue
1
Publisher
Plapiqui(UNS-Conicet)
Publisher Location
CAMINO LA CARRINDANGA, KM 7, C C 717, 8000 BAHIA BLANCA, ARGENTINA