Protein thermal stabilization in aqueous solutions of osmolytes.

Bruździak, Piotr; Panuszko, Aneta; Jourdan, Muriel; Stangret, Janusz

doi:10.18388/abp.2014_950

Cited by 14 publications

(19 citation statements)

References 26 publications

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“…There are several equations defined by the use of different symbols but all addressing the same issues. The issues are mainly solution structure, the change in such structure whenever an osmolyte or a macromolecule is introduced into any of such solution; the effect of the osmolytes on the macromolecular three dimensional (3-D) structure is often investigated using various biophysical instrument amenable to mainly biophysical studies [2]. There is also an attempt to link the interaction parameters to Kirkwood-Bulk integrals and m-value (this is the slope of the plot of free energy of folding to unfolding transition versus cosolvent concentration) [3][4][5][6][7].…”

Section: Introductionmentioning

confidence: 99%

“…There is also an attempt to link the interaction parameters to Kirkwood-Bulk integrals and m-value (this is the slope of the plot of free energy of folding to unfolding transition versus cosolvent concentration) [3][4][5][6][7]. The catalytic activities of the enzymes are also studied in the presence and absence of the osmolytes with the hope of understanding or establishing the effect of thermodynamic temperature increase in particular may be on the function of the enzyme [2,8]. There were theoretical studies in the past [3,9] all geared towards gaining theoretical insight into the solution structure and thermodynamic properties.…”

Section: Introductionmentioning

confidence: 99%

“…Most of the models are at the far end of biophysics with cognate biophysical methods. The hi-tech instruments for achieving the intended measurements are those for circular dichroism spectroscopy, infrared spectroscopy, differential scanning calorimetry, Fourier transform infrared spectroscopy etc [2]. An example of biochemical method is the assay of any enzyme whose velocity of action can be monitored using spectrophotometer of any kind that may be suitable.…”

Section: Introductionmentioning

confidence: 99%

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Theoretical Insight into Preferential Interaction Issues and Solution Structure, and Contentious Apparent Hydrated Molar Volume of Cosolute

Udema¹,

Onigbinde

2019

AJRB

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Background: There seems to be a mathematical or a conceptual error in an equation whose substitution into other equations for the determination of an apparent hydrated molar volume (V 1 ) of a cosolute leads to an incorrect answer. Objectives: The objectives are 1) To show theoretically that the preferential interaction parameter (PIP) is an extensive thermodynamic quantity, 2) rederive new equations and reexamine various equations related to solution structure, 3) apply derived equation for the determination of V 1 , and 4) determine m-values and cognate preferential interaction parameter (PIP).2 Results and Discussion: The investigation showed that equation linking chemical potential of osmolyte to solution structure is dimensionally invalid; PIP was seen as a thermodynamically extensive quantity. Equations for the graphical determination of V 1 of the osmolyte were derived. With ethanol alone, there were − m-value and + PIP; with aspirin alone, there were + m-value and − PIP. There was a change in sign in m-value with sucrose and ethanol/aspirin mixture, and a change in sign in PIP when the latter is taken as function of [ethanol]/[aspirin] and [sucrose]( ‫ܥ‬ ଷ ). Conclusion: A solution structure is as usual determined by either a relative excess or a deficit of the solution component either in the bulk or around the macromolecular surface domain; the PIP remains thermodynamically an extensive quantity. To be valid there is a need to introduce a reference standard molar concentration or activity to some equations in literature. The slope ߲ ൬from one of the equations seems to give a valid value for V 1 (V 1 is «1; γ ଷ is activity coefficient). A known destabiliser may behave as a stabiliser being excluded. Like ethanol, aspirin as cosolute is destabilising and opposed by sucrose.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Theoretical Insight into Preferential Interaction Issues and Solution Structure, and Contentious Apparent Hydrated Molar Volume of Cosolute

Udema¹,

Onigbinde

2019

AJRB

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“…Osmolytes are small organic molecules occurring naturally which have the ability to minimize osmotic stress. They stabilize the native state of proteins by raising the free energy of the unfolded state thereby driving the folding equilibrium toward natively folded conformations [15]. Osmolytes mainly include amino acids and their derivatives, polyols, sugars and methylamines.…”

Section: Introductionmentioning

confidence: 99%

“…Osmolytes mainly include amino acids and their derivatives, polyols, sugars and methylamines. Compounds such as glycine, N-methylglycine, N,N-dimethylglycine, N,N,N-trimethylglycine, trimethyl-N-oxide, polyethylene glycols, sucrose, trehalose, glycerol and many others also fall under this category and have been found to increase stability in several proteins[15–19]. Likewise, many compounds such as glycerol, sorbitol, sucrose, glycine, proline, betaine, sarcosine and trimethyl-N-amine have been found to be effective against protein aggregation [17, 19].…”

Section: Introductionmentioning

confidence: 99%

Synergistic Inhibition of Protein Fibrillation by Proline and Sorbitol: Biophysical Investigations

et al. 2016

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We report here interesting synergistic effects of proline and sorbitol, two well-known chemical chaperones, in the inhibition of fibrillation of two proteins, insulin and lysozyme. A combination of many biophysical techniques has been used to understand the structural morphology and modes of interaction of the chaperones with the proteins during fibrillation. Both the chaperones establish stronger polar interactions in the elongation and saturation stages of fibrillation compared to that in the native stage. However, when presented as a mixture, we also see contribution of hydrophobic interactions. Thus, a co-operative adjustment of polar and hydrophobic interactions between the chaperones and the protein surface seems to drive the synergistic effects in the fibrillation process. In insulin, this synergy is quantitatively similar in all the stages of the fibrillation process. These observations would have significant implications for understanding protein folding concepts, in general, and for designing combination therapies against protein fibrillation, in particular.

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Taurine as a water structure breaker and protein stabilizer

et al. 2017

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The enhancing effect on the water structure has been confirmed for most of the osmolytes exhibiting both stabilizing and destabilizing properties in regard to proteins. The presented work concerns osmolytes, which should be classified as “structure breaking” solutes: taurine and N,N,N-trimethyltaurine (TMT). Here, we combine FTIR spectroscopy, DSC calorimetry and DFT calculations to gain an insight into the interactions between osmolytes and two proteins: lysozyme and ubiquitin. Despite high structural similarity, both osmolytes exert different influence on protein stability: taurine is a stabilizer, TMT is a denaturant. We show also that taurine amino group interacts directly with the side chains of proteins, whereas TMT does not interact with proteins at all. Although two solutes weaken on average the structure of the surrounding water, their hydration spheres are different. Taurine is surrounded by two populations of water molecules: bonded with weak H-bonds around sulfonate group, and strongly bonded around amino group. The strong hydrogen-bonded network of water molecules around the amino group of taurine further improves properties of enhanced protein hydration sphere and stabilizes the native protein form. Direct interactions of this group with surface side chains provide a proper orientation of taurine and prevents the group from negative influence. The weakened hydration sphere of TMT breaks up the hydrogen-bonded network of water around the protein and destabilizes it. However, TMT at low concentration stabilize both proteins to a small extent. This effect can be attributed to an actual osmophobic effect which is overcome if the concentration increases.Electronic supplementary materialThe online version of this article (doi:10.1007/s00726-017-2499-x) contains supplementary material, which is available to authorized users.

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Protein thermal stabilization in aqueous solutions of osmolytes.

Cited by 14 publications

References 26 publications

Theoretical Insight into Preferential Interaction Issues and Solution Structure, and Contentious Apparent Hydrated Molar Volume of Cosolute

Theoretical Insight into Preferential Interaction Issues and Solution Structure, and Contentious Apparent Hydrated Molar Volume of Cosolute

Synergistic Inhibition of Protein Fibrillation by Proline and Sorbitol: Biophysical Investigations

Taurine as a water structure breaker and protein stabilizer

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