Molecular Interactions from the Experimental and Validation with Estimated Theoretical Sound Velocity

Palaniappan, L.; Nithiyanantham, S.

doi:10.1007/s42250-019-00091-w

Cited by 14 publications

(3 citation statements)

References 16 publications

(20 reference statements)

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“…These characterizations offer a valid interaction picture thereby elucidating role of pH on denaturation and role of cosolvent on renaturation. Such techniques are highly specific as regards the bulk nature of the system and are a well established approach for the study of molecular interactions [6][7][8][9]. Further the effects of pre-treatments, pH, additives, cosolvent etc are sharply reflected in the trend of observed ultrasonic parameters.…”

Section: Introductionmentioning

confidence: 99%

Affinity study of -lactalbumin nanoparticles in a mixed solvent environment using Laplace transform technique

Kavitha¹,

Palaniappan²

2022

Bull. Chem. Soc. Eth.

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ABSTRACT. Effect of pH and cosolvent on the stabilization of protein structure is a well established study in protein or food science. Of the various interesting applications of protein nanoparticles, making it as a drug or bioactive compound carrier is of vital importance. This application of protein nanoparticle demands the affinity priority of protein with the available components of the medium. The basis of such studies lies in the synthesis of such protein nanoparticles and their characterizations. Secondly the knowledge of priority in affinity of protein to a particular solvent is essential. On this basis, the present work deals with the ultrasonic analysis of hydophobic interactions exhibited by the α-lactalbumin nanoparticle synthesised by heat treatment using acetone as desolvating agent. In order to enrich the variations in hydrophobicity, pH and cosolvent (fructose) are included in the study. The results are compared with one of our earlier work and are interpreted in terms of the interactions existing among the components and the evolved discussions reveal that the bulk nature of the medium is controlled by the existing hydrophobicity interactions. Further, as a novel attempt, the preference of protein particle to interact with a particular solvent in mixed solvent environment is elucidated using Laplace transform technique. This approach is expected to torch light in protein science in fixing the most desirable solvent in mixed solvent environment. KEY WORDS: a-Lactalbumin, Fructose, Laplace Transform, Diffusion, Hydrophobic interactions Bull. Chem. Soc. Ethiop. 2021, 35(3), 659-668. DOI: https://dx.doi.org/10.4314/bcse.v35i3.16

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Section: Introductionmentioning

confidence: 99%

Affinity study of -lactalbumin nanoparticles in a mixed solvent environment using Laplace transform technique

Kavitha¹,

Palaniappan²

2022

Bull. Chem. Soc. Eth.

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“…Though the alcohol molecule is in a symmetric molecular environment the environment is not fully symmetric. This asymmetric environment by symmetric molecules is expected to interact differently with a polar molecule such as alcohol [12]. On this basis the present work is the thorough study on the molecular interaction process of aniline + m-xylene + isomeric butanol, using the sound velocity data.…”

Section: Introductionmentioning

confidence: 99%

Physico-chemical Studies of Isomeric Butanols in Aniline with m-Xylene

Palaniappan

Nithiyanantham²,

Murugesan

2020

Chemistry Africa

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The values of sound velocity, density and viscosity have been measured at 303 K in the ternary systems of aniline + m-xylene + n, sec, tert and iso-butanols. From these data, acoustical parameters such as molar volume, adiabatic compressibility, free length, free volume and internal pressure have been estimated using the standard relations. The results are interpreted in terms of molecular interaction between the components of the mixtures. The presence of weak dipoleinduced dipole interactions of larger magnitude is confirmed in the ternary systems. Of all the isomeric butanols, 1-ol, and especially 2-ol are found to be good structure makers that make the ternary complexes. In addition the possible interactions between the components are further confirmed by their excess values.

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“…The objective of the present work is to study the effect of heat pre-treatment and cosolvent on the hydrophobic interaction existing in the said system by using ultrasonic the bulk nature of the system and is a well-established approach for the study of molecular interactions (Swain and Priyadarshini 2010;Taulier et al 2005;Palaniappan and Nithyanandham 2019;Bahadur 2017). Further the effects of trend of observed ultrasonic parameters.…”

Section: Introductionmentioning

confidence: 99%

Hydrophobicity Character of A-lactalbumin Nanoparticles: An Ultrasonic Study

Kavitha¹,

Palaniappan²

2019

stj

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Effect of pH and cosolvent on the stabilization of protein structure is a well established study in protein or food science. Among the various applications of proteins, the use of protein nanoparticle as drug or bioactive compound carriers is the one which is of most interest to many diverse researchers. The synthesis of such protein nanoparticles and their characterization is of prior requirement for the realization of these drug or bioactive carriers. On this basis, the present work deals with the ultrasonic analysis of hydrophobic interactions exhibited by the a-lactalbumin nanoparticle synthesized by heat treatment using acetone as desolvating agent. In order to enrich the variations in hydrophobicity, heat or temperature and cosolvent (glucose) are included in the study. The results are interpreted in terms of the interactions existing among the components and the evolved discussions reveal the bulk nature of the medium is controlled by the existing hydrophobicity interactions. The obtained results indicate that the dependency of protein denaturation on heat and the strengthening of non- covalent interactions by the cosolvent and/or the steric exclusion effect can be attributed to the structural modifications of protein.

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Molecular Interactions from the Experimental and Validation with Estimated Theoretical Sound Velocity

Cited by 14 publications

References 16 publications

Affinity study of -lactalbumin nanoparticles in a mixed solvent environment using Laplace transform technique

Affinity study of -lactalbumin nanoparticles in a mixed solvent environment using Laplace transform technique

Physico-chemical Studies of Isomeric Butanols in Aniline with m-Xylene

Hydrophobicity Character of A-lactalbumin Nanoparticles: An Ultrasonic Study

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