DSC studies on bovine serum albumin denaturation Effects of ionic strength and SDS concentration

Giancola, Concetta; Sena, C. De; Fessas, Dimitrios; Graziano, Giuseppe; Barone, G.

doi:10.1016/s0141-8130(97)01159-8

Cited by 208 publications

(160 citation statements)

References 35 publications

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“…1, clearly displaying the LCST phase behavior. At pH = 7.0 and at moderate ionic strengths, the denaturation temperature of BSA is above 60 1C, [47][48][49] preventing the extension of the phase diagram to higher temperatures. We note that for temperatures higher than 45 1C, the dense phases became gel-like and the determined protein concentrations on the high density side of the binodal are smaller than those at lower temperatures.…”

Section: Binodal Of Lcst-llps For a Given Protein-salt Compositionmentioning

confidence: 99%

Kinetics of liquid–liquid phase separation in protein solutions exhibiting LCST phase behavior studied by time-resolved USAXS and VSANS

et al. 2016

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aWe study the kinetics of the liquid-liquid phase separation (LLPS) and its arrest in protein solutions exhibiting a lower critical solution temperature (LCST) phase behavior using the combination of ultrasmall angle X-ray scattering (USAXS) and very-small angle neutron scattering (VSANS). We employ a previously established model system consisting of bovine serum albumin (BSA) solutions with YCl 3 . We follow the phase transition from sub-second to 10 4 s upon an off-critical temperature jump. After a temperature jump, the USAXS profiles exhibit a peak that grows in intensity and shifts to lower q values

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Section: Binodal Of Lcst-llps For a Given Protein-salt Compositionmentioning

confidence: 99%

Kinetics of liquid–liquid phase separation in protein solutions exhibiting LCST phase behavior studied by time-resolved USAXS and VSANS

et al. 2016

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“…[4][5][6][7][8][9][10][11][12][13][14] The status of bovine serum albumin (BSA) during denaturation has been analyzed and confirmed using far-ultraviolet circular dichroisom. 13,14 Thermal analysis using differential scanning calorimetry (DSC) discloses the thermodynamic conditions under which denaturation occurs and quantifies the enthalpy of denaturation.…”

mentioning

confidence: 99%

“…[4][5][6][7][8]18 It has been reported that DSC studies of BSA reveal the thermodynamics of the protein associated with denaturation, specifically the change in specific heat and enthalpy near the denaturation temperature T d . [6][7][8] However, relatively less attention has been paid to k of BSA (k BSA ). 18 Therefore, we measured k of aqueous solutions of BSA (k sol ) by varying T and pH to determine how denaturation affects thermal transport in the solutions.…”

mentioning

confidence: 99%

Thermal conductivity of bovine serum albumin: A tool to probe denaturation of protein

Park

et al. 2011

Applied Physics Letters

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We demonstrate a strong correlation between denaturation of bovine serum albumin (BSA) and the thermal conductivity k of aqueous solutions of BSA. When denaturation of BSA began, k dropped significantly. These results suggest that k, i.e., the ability of a protein to transport passively applied thermal energy, can be exploited to probe the conformational dynamics of BSA and potentially of other proteins. The technique of protein analysis demonstrated in this work is expected to be useful in micro-total-analysis systems because it is easier to miniaturize and to integrate into a device than is conventional differential scanning calorimetry analysis.

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“…T max for the native protein depends on factors such as the ionic strength and the pH of the samples 17,18 and values ranging from 56 C to 86 C have been reported. [33][34][35][36] Under our experimental conditions, T max was around 66 C ( Fig. 5 and H-NMR spectrum of the poly(amidoamine)s. 35 or interferon 38 has improved the thermal stability of the proteins, PEG seemed to be inefficient when used to form non-covalent complexes.…”

Section: Interaction With Bsamentioning

confidence: 75%

Poly(amidoamine)s synthesis, characterisation and interaction with BSA

Dubois

Lavignac

2014

Polym. Chem.

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Cationic poly(amidoamine)s (PAAs) were synthesised and characterised by NMR and gel permeation chromatography. Their thermal properties were investigated using thermogravimetric analysis and differential scanning calorimetry. Although poly(amidoamine)s have been used as endosomolytic polymers for protein intracellular delivery, the interaction of the polymers with the proteins still need to be investigated. BSA was used as a model protein and complexation with the different poly(amidoamine) s was investigated using gel retardation assays, fluorescence spectroscopy and high sensitivity differential scanning calorimetry. Our results indicate that the thermal stability of BSA was affected upon interaction and complexation with the poly(amidoamine)s, however these interactions did not seem to modify the structure of the protein. Polymer flexibility seemed to favour polymer/protein complexation and promoted thermal stability.

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DSC studies on bovine serum albumin denaturation Effects of ionic strength and SDS concentration

Cited by 208 publications

References 35 publications

Kinetics of liquid–liquid phase separation in protein solutions exhibiting LCST phase behavior studied by time-resolved USAXS and VSANS

Kinetics of liquid–liquid phase separation in protein solutions exhibiting LCST phase behavior studied by time-resolved USAXS and VSANS

Thermal conductivity of bovine serum albumin: A tool to probe denaturation of protein

Poly(amidoamine)s synthesis, characterisation and interaction with BSA

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