Effect of Aqueous Alcohol Solutions on the Thermal Transition of Lysozyme:  A Calorimetric Study

Cinelli, Stefania; Onori, G.; Santucci, A.

doi:10.1021/jp971399p

Cited by 56 publications

(60 citation statements)

References 18 publications

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“…The thermal denaturation of lysozyme has been studied in TBA-water and ethanol-water mix-tures, finding that there is a relationship between the microstructure of the solvent and the conformation of the protein. 8 However, the authors suggested that the alcohols affected the conformation of protein via an indirect mechanism with structural reorganization of water and there was no direct interaction between the alcohols and the protein, 8 which was different from the conclusion from other reports. [3][4][5][6] The previous work from our group described thermodynamic properties of amino acids, the model compounds of protein, in several alcohol-water mixtures.…”

Section: Introductionmentioning

confidence: 85%

“…In the range 0 mol•L -1 ≤c TBA ≤2.5 mol•L -1 , the hydrodynamic radius of BSA exhibits an S type behavior, which is almost the same as the TBA concentration dependence of hydrodynamic radius of lysozyme. 26 On the basis of the thermal denaturation of lysozyme in TBA-water and ethanol-water mixtures, Onori 8 suggested that the net consequence of the effect of hydrophobic hydration was to enhance the solubility of nonpolar species and to disfavor their aggregation and that hydrophobic interactions at a concentration of hydrophobic groups lower than a critical concentration were repulsive and gave a destabilizing contribution to the native structure of protein. Thus, the attenuation of these interactions due to alcohol addition should favor clustering of hydrophobic groups and lead to a more compact conformation of protein.…”

Section: Conformational Change Of Bsa In Tba-water Mixturesmentioning

confidence: 99%

“…The above description was in agreement with the earlier work by spectroscopy on the conformational change of proteins in low concentrated alcohol-water mixtures. [3][4][5][6] However, the authors 8 suggested that the alcohols affected the conformation of protein via an indirect mechanism with structural reorganization of water and there was no direct interaction between the alcohols and the protein, which was different from the conclusions from other reports 3-6 and could not provide a consistent explanation for the anomalous behavior of hydrodynamic radius of lysozyme in TBA-water and ethanol-water mixtures. UV-vis absorption measurement is a simple method and applicable to explore the conformational change of protein.…”

Section: Conformational Change Of Bsa In Tba-water Mixturesmentioning

confidence: 99%

“…7,8 In spite of a large number of studies the mechanism of alcohols affecting the stability and solubility of proteins remains unresolved [3][4][5][6][7][8] due to the complex microstructure of the alcohol-water mixtures. [9][10][11][12][13][14][15] By far, little attention was paid to the relationship between the microstructure of alcohol-water mixtures and the conformation of proteins.…”

Section: Introductionmentioning

confidence: 99%

“…The TBA-water mixture is characterized by the anomalous physicochemical properties 9,10 and is considered as the typical compound to investigate the interaction of alcohols with proteins. [8][9][10][11][12][13][14][15] Recently, a variety of spectroscopic techniques including IR, 11 dynamic light scattering, 12 X-ray scattering 13 and neutron diffraction, 14 and theoretical approaches 15 have been used to reveal the microscopic structure of aqueous solutions of TBA and provide a new insight into the anomalous properties of the solutions at a molecule level. The thermal denaturation of lysozyme has been studied in TBA-water and ethanol-water mix-tures, finding that there is a relationship between the microstructure of the solvent and the conformation of the protein.…”

Section: Introductionmentioning

confidence: 99%

See 4 more Smart Citations

Influence of the Mixing State of tert‐Butyl Alcohol‐water Mixtures on the Conformation of Bovine Serum Albumin

Ma¹,

Xu²,

Xu³

et al. 2008

Chin. J. Chem.

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The hydrodynamic radii of bovine serum albumin (BSA) in TBA-water mixtures were determined by dynamic light scattering measurements and utilized to investigate the conformational change of BSA in TBA-water mixtures, together with the analysis of the fluorescence spectra and UV-vis absorption spectra of BSA. Meanwhile, static light scattering measurements were used to probe the mixing state of the binary mixtures of TBA-water and the ternary mixtures of BSA-TBA-water and its influence on the conformation of the protein. A close relationship between the mixing state of TBA-water mixtures and the conformation of BSA was observed. The mixing state of TBA-water mixture at a low concentration was characterized by the clathrate hydrate of TBA caged by water molecules and it was found that hydrophobic binding of TBA to nonpolar groups of BSA in general destabilized the native structure of the protein, however, addition of a small amount of TBA attenuated the hydrophobic interactions among nonpolar groups of the protein and promoted a more ordered conformation. The results clearly showed that clustering of TBA at a high concentration reduced the effectiveness on destabilization of the compact conformation of proteins.

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Section: Introductionmentioning

confidence: 85%

Section: Conformational Change Of Bsa In Tba-water Mixturesmentioning

confidence: 99%

Section: Conformational Change Of Bsa In Tba-water Mixturesmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Influence of the Mixing State of tert‐Butyl Alcohol‐water Mixtures on the Conformation of Bovine Serum Albumin

Ma¹,

Xu²,

Xu³

et al. 2008

Chin. J. Chem.

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Counteraction ability of TMAO toward different denaturing agents

et al. 2018

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Differential scanning calorimetry measurements performed on RNase A in aqueous binary solutions containing different concentrations of urea, tetramethylurea, guanidinium chloride, and guanidinium thiocyanate, and in aqueous ternary solutions, containing the same denaturants plus 1 M trimethylamine N-oxide, TMAO, demonstrate that the latter has a general counteracting ability at pH 7.0, but not at pH 4.0. Experimental data rule out the idea that counteraction originates from direct interactions between TMAO molecules and denaturing agents. A rationalization is provided on the basis of a theoretical approach grounded on the solvent-excluded volume effect, whose magnitude depends on the density of aqueous solutions.

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Protein–Protein Interactions in Complex Cosolvent Solutions

et al. 2007

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The effects of various kosmotropic and chaotropic cosolvents and salts on the intermolecular interaction potential of positively charged lysozyme is evaluated at varying protein concentrations by using synchrotron small-angle X-ray scattering in combination with liquid-state theoretical approaches. The experimentally derived static structure factors S(Q) obtained without and with added cosolvents and salts are analysed with a statistical mechanical model based on the Derjaguin-Landau-Verwey-Overbeek (DLVO) potential, which accounts for repulsive and attractive interactions between the protein molecules. Different cosolvents and salts influence the interactions between protein molecules differently as a result of changes in the hydration level or solvation, in charge screening, specific adsorption of the additives at the protein surface, or increased hydrophobic interactions. Intermolecular interaction effects are significant above protein concentrations of 1 wt %, and with increasing protein concentration, the repulsive nature of the intermolecular pair potential V(r) increases markedly. Kosmotropic cosolvents like glycerol and sucrose exhibit strong concentration-dependent effects on the interaction potential, leading to an increase of repulsive forces between the protein molecules at low to medium high osmolyte concentrations. Addition of trifluoroethanol exhibits a multiphasic effect on V(r) when changing its concentration. Salts like sodium chloride and potassium sulfate exhibit strong concentration-dependent changes of the interaction potential due to charge screening of the positively charged protein molecules. Guanidinium chloride (GdmCl) at low concentrations exhibits a similar charge-screening effect, resulting in increased attractive interactions between the protein molecules. At higher GdmCl concentrations, V(r) becomes more repulsive in nature due to the presence of high concentrations of Gdm(+) ions binding to the protein molecules. Our findings also imply that in calculations of thermodynamic properties of proteins in solution and cosolvent mixtures, activity coefficients may not generally be neglected in the concentration range above 1 wt % protein.

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Effect of Aqueous Alcohol Solutions on the Thermal Transition of Lysozyme: A Calorimetric Study

Cited by 56 publications

References 18 publications

Influence of the Mixing State of tert‐Butyl Alcohol‐water Mixtures on the Conformation of Bovine Serum Albumin

Influence of the Mixing State of tert‐Butyl Alcohol‐water Mixtures on the Conformation of Bovine Serum Albumin

Counteraction ability of TMAO toward different denaturing agents

Protein–Protein Interactions in Complex Cosolvent Solutions

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