2015
DOI: 10.1016/j.jct.2014.11.007
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Effect of temperature on solvation behaviour of diclofenac sodium salt in aqueous glycine and l-proline solutions

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Cited by 23 publications
(3 citation statements)
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“…To overcome this difficulty, the low mass analogues of proteins, such as amino acids, which mimic distinctive features of the protein framework, could be examined. Substantial research efforts have been extended in this regard. Since long, amino acids, such as l -proline and l -valine have been widely used as an excipient in nutraceuticals and pharmaceutical formulations. They enhance the solubility, stability, and bioavailability of the drugs, making them valuable in the development of various drug delivery platforms.…”
Section: Introductionmentioning
confidence: 99%
“…To overcome this difficulty, the low mass analogues of proteins, such as amino acids, which mimic distinctive features of the protein framework, could be examined. Substantial research efforts have been extended in this regard. Since long, amino acids, such as l -proline and l -valine have been widely used as an excipient in nutraceuticals and pharmaceutical formulations. They enhance the solubility, stability, and bioavailability of the drugs, making them valuable in the development of various drug delivery platforms.…”
Section: Introductionmentioning
confidence: 99%
“…1,2 A lot of interest have been evoked by the recognition of drugs activities in aqueous and nonaqueous solutions, which involve the interactions with biological membranes. 3−7 Physiologically, the consequences of a drug's action such as movement of the drug through the bloodstream, distributions, receptor binding, and lastly, desired actions involve an intricate mechanism 8 which can be perceived by knowing the thermodynamic behavior of such systems indicated by different noncovalent interactions. The stabilization of the native conformation of biological molecules (proteins) are associated with several noncovalent interactions encompassing hydrogen-bonding, electrostatic, and hydrophobic interactions.…”
Section: Introductionmentioning
confidence: 99%
“…In all the metabolic pathways or biological processes occurring inside the body, the drug–protein interactions have an important role. Modern drug discovery is dependent upon these interactions to reveal target proteins which are responsible for the pharmacological action by biological molecules. , A lot of interest have been evoked by the recognition of drugs activities in aqueous and nonaqueous solutions, which involve the interactions with biological membranes. Physiologically, the consequences of a drug’s action such as movement of the drug through the bloodstream, distributions, receptor binding, and lastly, desired actions involve an intricate mechanism which can be perceived by knowing the thermodynamic behavior of such systems indicated by different noncovalent interactions. The stabilization of the native conformation of biological molecules (proteins) are associated with several noncovalent interactions encompassing hydrogen-bonding, electrostatic, and hydrophobic interactions. , The properties such as solubility, hydration, and enzyme activity for the globular proteins are effected due to changes in water structure and solute–solvent interactions in the presence of solute; hydration, solubility, and the activity of enzymes are affected by the presence of these solutes. For a better understanding of these molecules in the medium, it is necessary to determine the state and functionality of the molecules in the medium. , To better illuminate these phenomena, several building blocks and model compounds of proteins (like amino acids/peptides) having low molar mass have been analyzed because it is not feasible to have direct thermodynamics studies on three-dimensional proteins having complex conformations.…”
Section: Introductionmentioning
confidence: 99%