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2017 ; 12
(2
): e0172208
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Selective inhibition of aggregation/fibrillation of bovine serum albumin by
osmolytes: Mechanistic and energetics insights
#MMPMID28207877
Dasgupta M
; Kishore N
PLoS One
2017[]; 12
(2
): e0172208
PMID28207877
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Bovine serum albumin (BSA) is an important transport protein of the blood and its
aggregation/fibrillation would adversely affect its transport ability leading to
metabolic disorder. Therefore, understanding the mechanism of
fibrillation/aggregation of BSA and design of suitable inhibitor molecules for
stabilizing its native conformation, are of utmost importance. The qualitative
and quantitative aspects of the effect of osmolytes (proline, hydroxyproline,
glycine betaine, sarcosine and sorbitol) on heat induced aggregation/fibrillation
of BSA at physiological pH (pH 7.4) have been studied employing a combination of
fluorescence spectroscopy, Rayleigh scattering, isothermal titration calorimetry
(ITC), dynamic light scattering (DLS) and transmission electron microscopy (TEM).
Formation of fibrils by BSA under the given conditions was confirmed from
increase in fluorescence emission intensities of Thioflavin T over a time period
of 600 minutes and TEM images. Absence of change in fluorescence emission
intensities of 8-Anilinonaphthalene-1-sulfonic acid (ANS) in presence of native
and aggregated BSA signify the absence of any amorphous aggregates. ITC results
have provided important insights on the energetics of interaction of these
osmolytes with different stages of the fibrillar aggregates of BSA, thereby
suggesting the possible modes/mechanism of inhibition of BSA fibrillation by
these osmolytes. The heats of interaction of the osmolytes with different stages
of fibrillation of BSA do not follow a trend, suggesting that the interactions of
stages of BSA aggregates are osmolyte specific. Among the osmolytes used here, we
found glycine betaine to be supporting and promoting the aggregation process
while hydroxyproline to be maximally efficient in suppressing the fibrillation
process of BSA, followed by sorbitol, sarcosine and proline in the following
order of their decreasing potency: Hydroxyproline> Sorbitol> Sarcosine> Proline>
Glycine betaine.
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