Ionic liquids (ILs) in aqueous solution can be used as tunable biomaterials to stabilize or destabilize proteins for a variety of biotechnological applications. By understanding how molecular interactions involving the ILs and proteins coordinate to stabilize or destabilize different protein structures it could be possible to design IL-based biomaterials for structure-specific protein stabilization. Numerous reports have investigated helix or sheet protein destabilization by ILs but studies on mixed-structure proteins are less common. This presentation will explore how different ILs affect the mixed-structure copper-binding proteins azurin, nitrite reductase, and laccase. The ILs include both imidazolium chloride ILs and amino acid-based ILs, and the investigative methods include protein unfolding thermodynamics measurements (from temperature-dependent IR, CD, and fluorescence spectroscopy), kinetics experiments (from temperature-jump and HDX techniques) and molecular dynamics simulations. The results elucidate how different ILs have different destabilization effects and mechanisms on the target proteins.<br/>

Different modes of destabilizing mixed-structure proteins by ionic liquids in aqueous solution

Macromolecular Chemistry: The Second Century

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ACS Spring 2020 National Meeting & Expo

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