Abstract

Ionic liquids (ILs) have been receiving much attention as solvents in various areas of biochemistry because of their various beneficial properties over the volatile solvents and ILs availability in myriad variants (perhaps as many as 108) owing to the possibility of paring one cation with several anions and vice-versa as well as formulations as zwitterions. Their potential as solvents lies in their tendency to offer both directional and non-directional forces toward a solute molecule. Because of these forces, ionic liquids easily undergo intermolecular interactions with a range of polar/non-polar solutes, including biomolecules such as proteins and DNA. The interaction of genomic species in aqueous/non-aqueous states assists in unraveling their structure and functioning, which have implications in various biomedical applications. The charge density of ionic liquids renders them hydrophilic and hydrophobic, which retain intact over long-range of temperatures. Their ability in stabilizing or destabilizing the 3D-structure of a protein or the double-helical structure of DNA has been assessed superior to the water and volatile organic solvents. The aptitude of an ion in influencing the structure and stability of a native protein depends on their ranking in the Hofmeister series. However, at several instances, a reverse Hofmeister ordering of ions and specific ion-solute interaction has been observed. The capability of an ionic liquid in terms of the tendency to promote the coiling/uncoiling of DNA structure is noted to rely on the basicity, electrostatic interaction, and hydrophobicity of the ionic liquid in question. Any change in the DNA's double-helical structure reflects a change in its melting temperature (Tm), compared to a standard buffer solution. These changes in DNA structure have implications in biosensor design and targeted drug-delivery in biomedical applications. In the current review, we have attempted to highlight various aspects of ionic liquids that influence the structure and properties of proteins and DNA. In short, the review will address the issues related to the origin and strength of intermolecular interactions, the effect of structural components, their nature, and the influence of temperature, pH, and additives on them.

Highlights

  • The energetics of a biological reaction/process change upon perturbing the solvent systems around it (Yancey et al, 1982)

  • The results indicated that the extraction ability of prepared aqueous biphasic systems (ABSs) depends inversely on the hydrogen bond donor basicity of anion with water

  • Compared to the dubious conclusions drawn from the ionic liquid-protein interactions owing to the structural variations, ionic liquid-Deoxyribonucleic acid (DNA) interactions are facile as the expected outcome of a particular ionic liquid on the structure and stability can be foreseen based on the available research

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Summary

Introduction

The energetics of a biological reaction/process change upon perturbing the solvent systems around it (Yancey et al, 1982). Molecular solvents, depending upon its nature, might offer various interactions ranging from dipole-dipole, electrostatic, van der Waals, hydrogen bonding, hydrophobic interactions, and so on. It is impossible to accommodate all the said interactions in a single molecular solvent. Despite its recognition as a universal solvent, offers only dipole-dipole, hydrogen bonding, and hydrophobic interactions for a solute. Almost all basic biological entities necessarily require a medium for their stabilization and functioning. Out of various basic biological candidates, we are, in particular, addressing the proteins and DNA in detail. As both proteins and DNA possess basic moieties, electrostatic, and hydrophobic centers, they require a medium that has all these interactions for their stabilization, functioning, long-term storage, and separation

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