Major
Chemistry
Anticipated Graduation Year
2024
Access Type
Open Access
Abstract
Our research focuses on studying the interaction between bovine serum albumin (BSA), a protein, and phospholipids, LPS, and DOTAP at varying concentrations. We utilize fluorescence spectroscopy to observe the quenching of the tryptophan residues in BSA, allowing us to explore the lipid binding sites in BSA. Through experimental studies, we determine the binding dissociation constant (Kd) and the number of fluorescent binding sites for lipids (n). Our findings provide insights into how different phospholipids, based on their structure, bind to BSA. Understanding these interactions can be used to further study various phospholipids using CIR to understand their molecular interactions with carrier proteins.
Faculty Mentors & Instructors
A.Sayeed,Dr.M.Ray
Creative Commons License
This work is licensed under a Creative Commons Attribution-No Derivative Works 3.0 License.
Fluorescence Spectroscopy Analysis of Phospholipids Bound to Bovine Serum Albumin
Our research focuses on studying the interaction between bovine serum albumin (BSA), a protein, and phospholipids, LPS, and DOTAP at varying concentrations. We utilize fluorescence spectroscopy to observe the quenching of the tryptophan residues in BSA, allowing us to explore the lipid binding sites in BSA. Through experimental studies, we determine the binding dissociation constant (Kd) and the number of fluorescent binding sites for lipids (n). Our findings provide insights into how different phospholipids, based on their structure, bind to BSA. Understanding these interactions can be used to further study various phospholipids using CIR to understand their molecular interactions with carrier proteins.