Date of Presentation
4-23-2024 9:00 AM
College
College of Science & Mathematics
Faculty Sponsor(s)
Dr. Gregory A. Caputo
Poster Abstract
Hen egg white lysozyme (Lyz) has been a well studied model system in biophysical investigations for decades. The protein is a small, primarily helical, highly soluble protein that is both commercially available and easily accessible. lonic liquids (ILs), often referred to as room-temperature ionic liquids or molten salts, have garnered great interest in the last 15-20 years as potential components of electrochemical devices or applications. More recently, the biocompatibility of these molecules has developed an increased interest in the field, especially considering that some IL species can stabilize biomolecular structures while other ILs strongly destabilize 3D structures. In this study, we used fluorescence spectroscopy to characterize the unfolding of lysozyme and the impact imidazolium-based ILs had on this process. The ILs 1-butyl-3-methylimidazolium chloride, 1-hexyl-3-methylimidazolium chloride, and 1-octyl-3-methylimidazolium chloride were first evaluated for their impacts alone, and subsequently on their ability to destabilize the lysozyme when denatured with Guanidinium HCl. Consistent with previous findings, the alkyl chain length had an impact on the destabilization potential of the ILs. Subsequent studies on the denaturation process in using thermal-induced denaturation, as well as quenching studies throughout the process, were also investigated to gain insight into the denaturation process. Overall, longer alkyl chain length ILs more strongly destabilize the lysozyme 3D structure.
Student Keywords
Lysozyme Stability, lonic Liquids
Disciplines
Chemistry
Document Type
Poster
Included in
Characterization of Lysozyme Stability in the Presence of lonic Liquids
Hen egg white lysozyme (Lyz) has been a well studied model system in biophysical investigations for decades. The protein is a small, primarily helical, highly soluble protein that is both commercially available and easily accessible. lonic liquids (ILs), often referred to as room-temperature ionic liquids or molten salts, have garnered great interest in the last 15-20 years as potential components of electrochemical devices or applications. More recently, the biocompatibility of these molecules has developed an increased interest in the field, especially considering that some IL species can stabilize biomolecular structures while other ILs strongly destabilize 3D structures. In this study, we used fluorescence spectroscopy to characterize the unfolding of lysozyme and the impact imidazolium-based ILs had on this process. The ILs 1-butyl-3-methylimidazolium chloride, 1-hexyl-3-methylimidazolium chloride, and 1-octyl-3-methylimidazolium chloride were first evaluated for their impacts alone, and subsequently on their ability to destabilize the lysozyme when denatured with Guanidinium HCl. Consistent with previous findings, the alkyl chain length had an impact on the destabilization potential of the ILs. Subsequent studies on the denaturation process in using thermal-induced denaturation, as well as quenching studies throughout the process, were also investigated to gain insight into the denaturation process. Overall, longer alkyl chain length ILs more strongly destabilize the lysozyme 3D structure.