Structural changes during the unfolding of Bovine serum albumin in the presence of urea: A small-angle neutron scattering study

Das, Amit Kumar; Читра, Р.; Choudhury, Rajul Ranjan; Ramanadham, M.

doi:10.1007/bf02704999

Cited by 22 publications

(18 citation statements)

References 24 publications

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“…The R g determined from the second moment of P(r), which is not as strongly impacted by the interparticle interference artifacts observable at low-q in some of the data sets, as would be the case for a traditional Guinier fit, 36 The SANS data collected in GdnHCl and the ILs at 25 °C are not consistent with a highly unfolded HSA 23 or an unfolded state of the related protein bovine serum albumin. 41,42 The difference between the initial, 25 °C SANS data (Figure 1A) and the data collected at 75 °C after the temperature ramp finished (Figure 1B) is dramatic. The transition between the two states can be seen in the SANS data shown in Figure 3, which are 5 min time slices of the event streams collected for each sample during the temperature ramp.…”

Section: ■ Resultsmentioning

confidence: 98%

Comparison of the Thermal Denaturing of Human Serum Albumin in the Presence of Guanidine Hydrochloride and 1-Butyl-3-methylimidazolium Ionic Liquids

Heller

2013

J. Phys. Chem. B

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The interaction of proteins with aqueous solutions of ionic liquids (ILs) has attracted considerable recent attention owing to the challenges of finding biocompatible water-free ILs. These systems remain of great interest because of the potential for using ILs as designer solvents for biocatalytic processes. Increasing evidence demonstrates that aqueous solutions of water-miscible ILs, such as the well-studied 1-alkyl-3-methylimidazolium ILs, disrupt the native fold of proteins and can drive the formation of non-native aggregates that could negatively impact catalytic function. Here, we present a study comparing the thermal unfolding of human serum albumin (HSA) in a 1 M solution of the protein denaturant guanidine hydrochloride with two 1 M aqueous solutions of 1-butyl-3-methylimidazolium ILs, namely the chloride and the acetate. Small-angle neutron scattering (SANS) measurements found qualitative agreement between the thermally driven unfolding process for the three denaturants, as well as with a Tris buffer solution. HSA irreversibly aggregates and unfolds in the three denaturant solutions upon heating to temperatures below that required to drive the same process in a simple Tris buffer solution. The results reveal subtle differences in the interaction of the ILs and guanidine hydrochloride with the protein, although the final states of the protein were similar in all cases. The results indicate that the ions of water-miscible ILs and guanidine hydrochloride have specific roles in disrupting protein structure and driving aggregation. The experimental approach employed has the potential to provide new insights into protein interactions with ionic liquids that may aid in the search for more biocompatible ionic liquids.

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Section: ■ Resultsmentioning

confidence: 98%

Comparison of the Thermal Denaturing of Human Serum Albumin in the Presence of Guanidine Hydrochloride and 1-Butyl-3-methylimidazolium Ionic Liquids

Heller

2013

J. Phys. Chem. B

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“…Recall that from the TEM and AFM pictures in Fig. 1 we estimated the average length and diameter of the filamentous BSA-Pas, l E 150 nm and d E 8 nm, and it is known 44 that a single denatured BSA molecule can be assumed to be an ellipsoid of a prolate shape with the minor axis equal to 1.73 nm and the major axis equal to 5.39 nm. Then, the major axis (5.39 nm) is comparable to the diameter (8 nm), and the minor axis (1.73 nm) times N agg is equal to 292 nm, which is also comparable to the estimated length (150 nm).…”

Section: Characterization Of the Bsa-pasmentioning

confidence: 99%

Stability and gelation behavior of bovine serum albumin pre-aggregates in the presence of calcium chloride

Arosio

Podolskaya

et al. 2012

Phys. Chem. Chem. Phys.

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We study, using wide-angle and small-angle light scattering techniques, the stability and aggregation/gelation behaviors of denatured filamentous bovine serum albumin pre-aggregates (BSA-PAs), induced by CaCl(2). It is observed that transparent filamentous gels can be formed not only at low CaCl(2) concentrations but also at high CaCl(2) concentrations, while turbid gels are obtained at intermediate CaCl(2) concentrations. Although the filamentous gels at low CaCl(2) concentrations and the turbid gels at intermediate CaCl(2) concentrations are consistent with the literature observations, the filamentous gels at high CaCl(2) concentrations have to be explained by different mechanisms. The latter is attributed to the repulsive hydration interactions originating from increased surface dipoles generated by counterion binding. Since such surface dipole-induced hydration is very short-range and occurs mainly on charged or polar patches of proteins (thus protected from aggregation), the aggregation of the filamentous BSA-PAs at hydrophobic patches at the two ends is still possible, leading to formation of the filamentous gels.

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“…34 The secondary structure purportedly contains roughly 67% a-helix structure. 35 The tertiary structure consists of nine loops stabilized by 17 internal disulfide bonds between 34 cysteine residues, resulting in three primary domains, each containing one small and two large loops. These disulfide bridges are the basis for the compact heart-shaped (equilateral triangle) structure.…”

Section: Introductionmentioning

confidence: 99%

Morphological effect of gold nanoparticles on the adsorption of bovine serum albumin

Chaudhary

Gupta

Khan

et al. 2014

Phys. Chem. Chem. Phys.

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Various properties of gold nanoparticles (GNPs) are found to play crucial roles in their biological activity. Among them, the morphology and surface chemistry are extremely important. This is because of differences in surface energies of various crystal facets arising from a large fraction of edges, corners and vertices. In the present work, we provide a comparative study on the adsorption and binding affinities of bovine serum albumin (BSA) onto triangular gold nanoplates (TGNP) and gold nanorods (GNR). The results were compared with similar size of both CTAB and citrate stabilized spherical GNPs. Our data suggested stronger binding of BSA on citrate stabilized spherical GNPs whereas TGNP shows the weakest binding among all the GNPs. A blue shift of approximately 20 nm in tryptophan fluorescence was observed for all CTAB stabilized GNPs, indicating the local dielectric changes surrounding the tryptophan residue. Loss of the secondary structure was also observed for all CTAB stabilized GNPs. No spectral shift was observed for citrate stabilized spherical GNPs though maximum quenching of fluorescence and minimum structural loss was observed. With the help of molecular simulation recently developed by our group, a binding model is proposed to explain all the above experimental results.

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Structural changes during the unfolding of Bovine serum albumin in the presence of urea: A small-angle neutron scattering study

Cited by 22 publications

References 24 publications

Comparison of the Thermal Denaturing of Human Serum Albumin in the Presence of Guanidine Hydrochloride and 1-Butyl-3-methylimidazolium Ionic Liquids

Comparison of the Thermal Denaturing of Human Serum Albumin in the Presence of Guanidine Hydrochloride and 1-Butyl-3-methylimidazolium Ionic Liquids

Stability and gelation behavior of bovine serum albumin pre-aggregates in the presence of calcium chloride

Morphological effect of gold nanoparticles on the adsorption of bovine serum albumin

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