A better understanding of how molecules interact in aqueous solutions has ramifications across biochemistry and biology. However, because classical physical laws assume that all ions are point charges (to name just one approximation), and because there is as yet no complete picture of how water solvates different kinds of solute surfaces, this area of aqueous supramolecular chemistry is replete with open questions. Our main approach to this problem has been to synthesize a series of water-soluble hosts that possess a well-defined, non-polar pocket. En masse these cavitand hosts have allowed us to probe both the hydrophobic effect and the Hofmeister effect. Concomitantly, the properties of these hosts and their corresponding self-assembled capsules have allowed us to, for example, build systems that function as yoctoliter (10–24 L) reaction vessels, or engender novel separation protocols. This presentation will focus on our recent results that follow these different lines of thought.1 Our hydrophobic and Hofmeister effect studies with model systems have most recently served as a foundation to probe how ions interact with proteins. Thus, this presentation will also discuss recent work looking at how salts affect the properties of the protein ubiquitin.2 Specifically, where ions interact with ubiquitin, and what the ramifications of these interactions are as a function of pH.

Probing and harnessing non-covalent interactions in water: From models hosts to proteins

ACS Spring Meeting 2021

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