Hydrotrope-Induced Micellar Phase of Sodium Dodecyl Slfate as New Detergent for Extraction and Stabilization of Proteins

Starova, Viktoriia S.; Kulichenko, S. A.

doi:10.23939/chcht12.02.196

Cited by 2 publications

(5 citation statements)

References 6 publications

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“…The impact of ATP binding thus shares some features with the behavior of ligand binding to stabilize protein structure, − even though the binding of ATPs is generally nonspecific. This mechanism is apparently distinct from the hydrotrope action which requires formation of micellar assembly to encapsulate protein . Moreover, the effects on the structural stability of the vulnerable region should be mainly attributed to the directly bound ATPs (∼70% of the accumulated ATPs), while the indirectly bound ATPs seems to be redundant.…”

Section: Results and Discussionmentioning

confidence: 96%

“…This mechanism is apparently distinct from the hydrotrope action which requires formation of micellar assembly to encapsulate protein. 20 Moreover, the effects on the structural stability of the vulnerable region should be mainly attributed to the directly bound ATPs (∼70% of the accumulated ATPs), while the indirectly bound ATPs seems to be redundant. Thus, a lower than physiological concentration of ATPs may be sufficient to realize protein protection.…”

Section: Results and Discussionmentioning

confidence: 99%

“… 17 − 19 The other is hydrotrope, e.g., sodium xylene sulfonate (NaXS), which forms complete micellar assembly to encapsulate protein to improve its solubility. 4 , 20 For both types of mechanisms, a high cosolvent concentration of up to ∼1000 mM is required to effectively solubilize proteins. By contrast, ATP at concentrations of less than 10 mM can effectively stabilize proteins.…”

Section: Introductionmentioning

confidence: 99%

“…To date, the mechanisms of natural cosolvent can be roughly categorized into two types. The first is osmolyte, e.g., trimethylamine N -oxide (TMAO), which indirectly enhances protein stability by altering the bulk water structure. − The other is hydrotrope, e.g., sodium xylene sulfonate (NaXS), which forms complete micellar assembly to encapsulate protein to improve its solubility. , For both types of mechanisms, a high cosolvent concentration of up to ∼1000 mM is required to effectively solubilize proteins. By contrast, ATP at concentrations of less than 10 mM can effectively stabilize proteins.…”

Section: Introductionmentioning

confidence: 99%

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ATP Can Efficiently Stabilize Protein through a Unique Mechanism

Lao

et al. 2021

JACS Au

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Recent experiments suggested that ATP can effectively stabilize protein structure and inhibit protein aggregation when its concentration is less than 10 mM, which is significantly lower than cosolvent concentrations required in conventional mechanisms. The ultrahigh efficiency of ATP suggests a unique mechanism that is fundamentally different from previous models of cosolvents. In this work, we used molecular dynamics simulation and experiments to study the interactions of ATPs with three proteins: lysozyme, ubiquitin, and malate dehydrogenase. ATP tends to bind to the surface regions with high flexibility and high degree of hydration. These regions are also vulnerable to thermal perturbations. The bound ATPs further assemble into ATP clusters mediated by Mg 2+ and Na + ions. More interestingly, in Mg 2+ -free ATP solution, Na + at higher concentration (150 mM under physiological conditions) can similarly mediate the formation of the ATP cluster on protein. The ATP cluster can effectively reduce the fluctuations of the vulnerable region and thus stabilize the protein against thermal perturbations. Both ATP binding and the considerable improvement of thermal stability of ATP-bound protein were verified by experiments.

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Section: Results and Discussionmentioning

confidence: 96%

Section: Results and Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

ATP Can Efficiently Stabilize Protein through a Unique Mechanism

Lao

et al. 2021

JACS Au

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“…The red region corresponding to these top residues can be thought of as the main region for ATP enrichment. As a comparison, the typical hydrotropes are generally considered to form complete micellar assembly encapsulating protein to enhance its solubility, − in which case the binding counts of the surface residues should be homogeneous. It should be noted that the same enrichment phenomenon of ATP also appears in the other two proteins (Figure a,b).…”

Section: Resultsmentioning

confidence: 99%

Mechanistic Insight on General Protein-Binding Ability of ATP and the Impacts of Arginine Residues

2022

J. Phys. Chem. B

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Recent experiments suggested that adenosine triphosphate (ATP) can regulate liquid–liquid phase separation (LLPS) of various proteins and inhibit protein aggregations at its physiological concentration, which is highly correlated with the nonspecific interactions of ATP to a wide variety of proteins. However, the mechanism underlying the general binding capability of ATP largely remains unclear. In this work, we used molecular dynamics simulation to study the binding of ATPs to three proteins with distinct net charges: TDP-43 NTD (−7 e), TAF15-RRM (0 e), HWEL (+8 e). Negatively charged ATP exhibits a strong trend to accumulate around all of these proteins. While only a fraction of the accumulated ATPs directly binds to the limited regions of the protein surface, additional ATPs indirectly bind to proteins by aggregating into ATP clusters. Hence, the proportion of the directly bound ATPs in the clusters as well as their binding regions can be adjusted in response to different proteins, which makes ATP well adapted to a variety of proteins. Moreover, our results suggest that ATP tightly binds to Arg with high affinity, and Arg dominates the direct binding of ATP. Meanwhile, Arg also affects the self-association of accumulated ATPs. The size of the ATP cluster is effectively regulated by the distribution of Arg. Considering the ubiquity of Arg in proteins, our findings are helpful to understand the general binding capability of ATP.

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Hydrotrope-Induced Micellar Phase of Sodium Dodecyl Slfate as New Detergent for Extraction and Stabilization of Proteins

Cited by 2 publications

References 6 publications

ATP Can Efficiently Stabilize Protein through a Unique Mechanism

ATP Can Efficiently Stabilize Protein through a Unique Mechanism

Mechanistic Insight on General Protein-Binding Ability of ATP and the Impacts of Arginine Residues

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