<br/>Hydrotropes are co-solvents capable of solubilizing hydrophobic entities in an aqueous medium. Recent experiments have shown that adenosine triphosphate (ATP), besides providing energy for cellular processes, also serves as a biological hydrotrope to destabilize protein aggregates. Herein, a multi-instrumental approach including lower critical solution temperature (LCST), NMR and FTIR were carried out to elucidate the underlying molecular mechanism of the ATP-macromolecule interactions. To do so, ATP is dissected into its subgroups to investigate the effects of adenine, adenosine, and the triphosphate in comparison to ATP on thermoresponsive macromolecules. Namely, poly(N-isopropylacrylamide) (PNIPAM) and poly (N,N-diethylacrylamide) (PDEA) macromolecules are employed, that have been widely used as a simple model of proteins. Our results show that the influence of the ATP subgroups on the macromolecules is highly pH dependent. At neutral solutions (pH 6 - 8.5), adenine and adenosine only slightly influence the solubility of macromolecules, whereas the ATP or triphosphate group act as a salting-out agents. This latter observation is in sharp contrast to the expected hydrotrope behavior of ATP molecule. Moreover, the FTIR and NMR measurements do not indicate a specific strong interaction between ATP and macromolecules. As such, electrostatic interactions should dominate the influence of ATP on aqueous macromolecule solutions.

ATP can act as a stabilizer for neutral macromolecules

Fall 2022 abstracts, posters, and presentations will launch in mid-September.

ACS Fall 2022

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.