Overview of the “Ionic Liquids meet Biomolecules” session at the 19th international IUPAB and 11th EBSA congress

Abstract

Room temperature ionic liquids (ILs) (Welton 1999) are a vast class of ionic systems consisting of an organic cation and either an organic or inorganic anion, whose melting temperature falls below the conventional limit of 100°C, making these compounds liquid at or near room temperature. The thermal and chemical stability of these systems make them the basis of what is called Bgreen chemistry^ (Earle and Seddon 2000). Several biochemical studies, however, have highlighted their potential toxicity to organisms, a toxicity which, in turn, is also a measure of their affinity for bio-molecules. This property has stimulated several chemical-physical studies on the interaction between ILs and basic biological systems. In recent decades, it has been observed that selected ILs are able: (1) to kill bacteria and cancer cells while leaving eukaryotic healthy cells almost unaffected; (2) to extract, purify and even preserve DNA at ambient temperature; (3) to stabilize proteins and enzymes; (4) to either favour or prevent protein amyloidogenesis; (5) to penetrate and eventually disrupt biomembranes via extended poration; and (6) to dissolve polysaccharides and cellulose. A recent overview of the subject is reported in two reviews authored by Benedetto and Ballone (2016a, b).The aim of the BIonic Liquid meet Biomolecules^session of the IUPAB-EBSA congress was to present an up-to-date overview of this new and intriguing subject of research which has potential applications in several fields, ranging from biomedicine, pharmacology, and material science to bionanotechnologies.Pannuru Venkatesu (University of Delhi, India) focuses on the interaction between ionic liquids and proteins (Meena et al. 2016;Jha and Venkatesu 2016), arguing that studies of interaction between proteins and different ILs in aqueous solution are comparatively more important than those in pure ILs. The results of these investigations suggest that the ILwater-protein interaction is a complex balance of different contributions by the different components, which is not possible to predict a priori. There is sufficient evidence in the literature to lead to the conclusion that the interaction between proteins and ILs depends on the protein as well as on the cations and anions present in the ILs.Antonio Benedetto (University College Dublin, Ireland, and Paul Scherrer Institut, Switzerland) presents results from joint experimental and computational studies on the interaction between ILs and (model) biomembranes (Benedetto 2017;Benedetto et al. 2015, Benedetto et al. 2014. Combining neutron scattering and computer simulations these studies show how it is possible to describe the mechanisms of interaction at the molecular level: IL cations penetrate the biomembrane, finding a preferential location between the tails and the heads of the phospholipids. The penetration is driven by the Coulombic attraction between the IL cations and one of the most electronegative oxygen atoms in the phospholipid heads, and is stabilized by dispersion forces between the lipids and th...

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