Priyanka bhukya | International Journal of Chemical Synthesis and Chemical Reactions | Vol 12, Issue 02 | ISSN: 2582-5917
Abstract
The acoustical and viscometric properties of L-Alanine (neutral, nonpolar) and L-Arginine (basic, charged) in 10% aqueous glycerol have been investigated over a concentration range of 0.01 to 0.1 mol·kg⁻¹ at temperatures T = 293.15, 298.15, 303.15, 308.15, 313.15, and 318.15 K under atmospheric pressure. Experimental measurements of ultrasonic velocity (µ), density (ρ), and viscosity (η) have been used to derive adiabatic compressibility (), apparent molar volume (Φv), partial molar volume (Φ°v), relative viscosity (η/η₀), and solvation number (ns), Transfer partial molar volume (ΔΦ°v) and transfer partial molar compressibility (ΔΦ°k) from pure water to 10% aqueous glycerol have also been determined for both amino acids at each temperature. L-Arginine exhibited higher ultrasonic velocity values and greater decrease in adiabatic compressibility compared to L-Alanine, reflecting the stronger molecular interactions arising from its positively charged guanidinium side chain. The relative viscosity (η/η₀) values greater than unity for both amino acids confirm strong solute-solvent interactions in 10% aqueous glycerol, with L-Arginine exhibiting higher relative viscosity values than L-Alanine throughout the investigated concentration and temperature range, attributed to the stronger interactions arising from its positively charged guanidinium side chain. The solvation numbers obtained from adiabatic compressibility data indicate a larger solvation sphere around L-Arginine molecules, reflecting stronger solvophilic hydration due to electrostatic interactions of the guanidinium group with surrounding solvent molecules. The transfer partial molar compressibility () values were found to be negative for L-Arginine and positive for L-Alanine across the entire temperature range investigated. This contrasting behavior clearly demonstrates the differential effect of glycerol on the two amino acids — glycerol strengthens and rigidifies the hydration shell of L-Arginine through strong hydrogen bonding interactions with its charged guanidinium group, while it weakens and disrupts the hydration shell of L-Alanine due to the weaker affinity of glycerol for its nonpolar methyl side chain. The results provide clear evidence for the dominant role of side chain polarity and charge in governing the solvation behavior and molecular interactions of amino acids in aqueous glycerol medium, with implications for understanding protein stabilization mechanisms in polyol-containing biological and pharmaceutical systems.
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How to cite this article
@article{bhukyaP2026,
author = {Priyanka bhukya},
title = {Comparative Acoustical and Viscometric Study Of L-Alanine And L-Arginine in Aqueous Glycerol Medium: Effect of Side Chain Polarity and Charge On Molecular Interactions},
journal = {International Journal of Chemical Synthesis and Chemical Reactions},
year = {2026},
volume = {12},
number = {02},
issn = {2582-5917},
url = {https://journalspub.com/publication/ijcscr/article=28153}
}