University of Tennessee at Chattanooga
Place of Publication
High-density lipoprotein function is essential for the healthy processing of fats in the blood. The function of these proteins is determined by their conformational structure of chains of amino acids. Certain ionic liquids have been shown to interact with individual amino acids to affect the tertiary shape of the protein. These interactions can disrupt the native hydrogen bonds between amino acids which can either promote folding or denaturing of the protein. Our work focused on apoA-1, a high-density lipoprotein that binds to cholesterol for efflux from the body. We studied this protein in different ion-based liquids with sodium, chloride, and 1-ethly-3-methylimidazolium (EMIM). The different solutions will be studied at different concentrations in water. This work will be done using molecular dynamic simulations of apoA-1 immersed in solution. Our simulations revealed which ions promote folding and which would be potential candidates for making solutions that stabilize apoA-1. The systems with sodium cations and others with chloride anions in solution reveal the effects of charge on the shape of the protein. EMIM cation with chloride counter anions in solutions shows that as the solvent concentration increases, the protein folds unstably but maintains its native secondary structures.
Chemistry and Physics Undergraduate Research Program Westbrook Scholarship Luis Sanchez-Diaz PhD Jisook Kim PhD
B. S.; An honors thesis submitted to the faculty of the University of Tennessee at Chattanooga in partial fulfillment of the requirements of the degree of Bachelor of Science.
High density lipoproteins
Smith, Benjamin, "Molecular dynamics simulations of apolipoprotein A1 in ionic liquids" (2020). Honors Theses.