Date of Presentation
4-23-2024 9:00 AM
College
College of Science & Mathematics
Faculty Sponsor(s)
Dr. Timothy D. Vaden
Poster Abstract
Azurin is a mixed-structure redox protein involved in bacterial denitrification. Previous studies have shown that azurin is destabilized by imidazolium chloride ionic liquids (ImCl ILs) that can form micelles in aqueous solution, likely by micellar encapsulation. In these ImCl ILs the micelles form from the imidazolium cations. A relatively new class of ionic liquids is fatty acid ionic liquids (FAILs), in which the anion is a fatty acid. In FAILs micelles can form from the fatty acid anions. This presentation presents the results of a thermal unfolding study of azurin in the presence of FAILs in solution. The FAILs tetramethylguanidinium decanoate and choline decanoate both strongly destabilize azurin when present above their critical micelle concentrations, while decanoic acid alone does not affect azurin (at the same concentration). The results point to the special nature of the FAILs and their interactions with the azurin structure and may be related to how the protein is encapsulated by FAIL micelles.
Student Keywords
Thermal Destabilization, Azurin, Fatty Acid Ionic Liquids, Chemistry
Disciplines
Chemistry
Document Type
Poster
Included in
Thermal Destabilization of Azurin by Fatty Acid Ionic Liquids
Azurin is a mixed-structure redox protein involved in bacterial denitrification. Previous studies have shown that azurin is destabilized by imidazolium chloride ionic liquids (ImCl ILs) that can form micelles in aqueous solution, likely by micellar encapsulation. In these ImCl ILs the micelles form from the imidazolium cations. A relatively new class of ionic liquids is fatty acid ionic liquids (FAILs), in which the anion is a fatty acid. In FAILs micelles can form from the fatty acid anions. This presentation presents the results of a thermal unfolding study of azurin in the presence of FAILs in solution. The FAILs tetramethylguanidinium decanoate and choline decanoate both strongly destabilize azurin when present above their critical micelle concentrations, while decanoic acid alone does not affect azurin (at the same concentration). The results point to the special nature of the FAILs and their interactions with the azurin structure and may be related to how the protein is encapsulated by FAIL micelles.