Mode of action of betaine on some amino acids and globular proteins: Thermodynamic considerations

Thoppil, Anu A.; Judy, Eva; Kishore, Nand

doi:10.1016/j.jct.2017.03.025

Cited by 10 publications

(10 citation statements)

References 38 publications

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“… a References and . b Reference . Standard uncertainties ( u ) are u ( T ) = ±0.01 K and u ( p ) = ±1 kPa. …”

Section: Resultsmentioning

confidence: 99%

“…The group contribution of glycine and glycyl peptides can be obtained by using the following equation ,, where ( V 2,m ° ) i is the contribution to the partial molar volume of a solute of a group type i and n i is denoted as the number of i th groups. All of the compounds along with their standard partial molar volumes in water, reported in earlier studies , and in the aqueous mixture of (DTAB + sorbitol), are listed in Table .…”

Section: Resultsmentioning

confidence: 99%

“…The group contribution of glycine and glycyl peptides can be obtained by using the following equation 18,22,31 V nV ( ) ( )…”

Section: Resultsmentioning

confidence: 99%

“…In this work, we have chosen some homopeptides as building blocks of proteins and studied their interactions with the mixture of (DTAB + sorbitol). The interactions of various amino acids and peptides in different solvents have provided valuable information about solute–solvent interactions. ,− Further, the work has been extended to the interaction of the mixture with the model protein hen egg white lysozyme. In order to understand whether the effect of osmolyte on the protein is direct or mediated via interaction with DTAB, efforts have been made to understand the interaction of the osmolyte with the monomers and micelles of the surfactant.…”

Section: Introductionmentioning

confidence: 99%

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Physicochemical Insights into the Stabilization of Stressed Lysozyme and Glycine Homopeptides by Sorbitol

Ghosh

Kishore

2018

J. Phys. Chem. B

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Understanding the mode of action of osmolytes on the protein with and without stressed conditions still requires experimental proof. In this direction, we have studied the interactions of a model protein hen egg white lysozyme (HEWL) and some homopeptides with sorbitol and a mixture of [dodecyltrimethylammonium bromide (DTAB) + sorbitol] by using a combination of high sensitivity calorimetry, density, sound velocity, and conductivity measurements with spectroscopic support. The physical chemistry underlying these interactions has been addressed on the basis of the energetics of interactions and other physicochemical properties. These results have highlighted that, even though the number of -CONH groups increases in higher homopeptides, the hydrophobic effect of - CH groups in the peptides dominates. Further, the counteraction of the deleterious effects of DTAB by sorbitol is due to the strengthened DTAB-sorbitol interactions rather than the indirect effect of the osmolyte via preferential exclusion. The results provide insights into the nature of interactions of the protein as well as some of the building blocks with the (DTAB + osmolyte) mixture which helped in understanding the mode of action of the osmolyte. Detailed physicochemical insights into the mode of action of stress counteracting agents on the protein and its destabilizer are needed to develop strategies to achieve optimum stability and activity of proteins under such conditions.

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“… a References and . b Reference . Standard uncertainties ( u ) are u ( T ) = ±0.01 K and u ( p ) = ±1 kPa. …”

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

“…The group contribution of glycine and glycyl peptides can be obtained by using the following equation 18,22,31 V nV ( ) ( )…”

Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Physicochemical Insights into the Stabilization of Stressed Lysozyme and Glycine Homopeptides by Sorbitol

Ghosh

Kishore

2018

J. Phys. Chem. B

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“…The functional properties of protein molecules depend upon their three dimensional structure which arises due to a particular sequence of amino acids (hereafter written as AA) in a polypeptide chain. All AAs exists as zwitterionic species in aqueous solutions [ 3 ], thus their thermodynamic properties in a variety of media can provide valuable information about the stability and denaturation of proteins [ 4 – 16 ]. Recently, Lomesh and Kumar [ 17 , 18 ] have reported the volumetric and acoustic properties of glycine, diglycine, l -alanine and l -phenylalanine in water and in 0.1 mol·kg −1 aqueous citric acid at different temperatures.…”

Section: Introductionmentioning

confidence: 99%

Volumetric Investigations on Molecular Interactions of Glycine/l-alanine in Aqueous Citric Acid Solutions at Different Temperatures

Patyar

Kaur

2018

J Solution Chem

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Apparent molar volumes of glycine/l-alanine in water and in aqueous citric acid (CA) solutions of varying concentrations, i.e. (0.05, 0.10, 0.20, 0.30, 0.40 and 0.50) mol·kg−1 were determined from density measurements at temperatures T = (288.15, 298.15, 308.15, 310.15 and 318.15) K and at atmospheric pressure. Limiting partial molar volumes and their corresponding partial molar volumes of transfer have been calculated from the data. The negative values obtained for glycine/l-alanine from water to aqueous CA solutions indicate the dominance of hydrophilic–hydrophobic/hydrophobic–hydrophilic and hydrophobic–hydrophobic interactions over ion/hydrophilic–dipolar interactions. Further, pair and triplet interaction coefficients, i.e. along with hydration number have also been calculated. The effect of temperature on the volumetric properties of glycine/l-alanine in water and in aqueous CA solutions has been determined from the limiting partial molar expansibilities and their second-order derivative . The apparent specific volumes for glycine and l-alanine tend to approach sweet taste behavior both in the presence of water and in aqueous CA solutions. The values for glycine/l-alanine increase with increase in concentration of CA at all temperatures studied. This reveals that CA helps in enhancing the sweet taste behavior of glycine/l-alanine which also supports the dominance of hydrophobic–hydrophobic interactions.Electronic supplementary materialThe online version of this article (10.1007/s10953-018-0829-6) contains supplementary material, which is available to authorized users.

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Influence of humectants on the thermotropic behaviour and nanostructure of fully hydrated lecithin bilayers

Moore²,

Thompson³

et al. 2022

Chemistry and Physics of Lipids

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Mode of action of betaine on some amino acids and globular proteins: Thermodynamic considerations

Cited by 10 publications

References 38 publications

Physicochemical Insights into the Stabilization of Stressed Lysozyme and Glycine Homopeptides by Sorbitol

Physicochemical Insights into the Stabilization of Stressed Lysozyme and Glycine Homopeptides by Sorbitol

Volumetric Investigations on Molecular Interactions of Glycine/l-alanine in Aqueous Citric Acid Solutions at Different Temperatures

Influence of humectants on the thermotropic behaviour and nanostructure of fully hydrated lecithin bilayers

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