Celebrating Scholarship and Creativity Day (2018-)
Document Type
Poster
Publication Date
5-1-2025
Disciplines
Biochemistry | Biochemistry, Biophysics, and Structural Biology | Other Biochemistry, Biophysics, and Structural Biology
Advisor
Md. Fazal PhD
Abstract
Nanoparticles are particles ranging from 1-100 nanometers in size. Most nanoparticles, upon contact with biological matrices, are immediately coated with proteins, forming the protein corona, which can alter the structure and function of proteins. Despite the tremendous advancement of nanotechnology over the last decade, the interactions of nanoparticles with proteins are not well characterized. This project investigates the effect of glycation on the binding interactions of HSA, the most abundant protein in human blood, with silver nanoparticles using various spectroscopic techniques. This is important because in diabetic patients, HSA is exposed to high concentrations of glucose over extended periods of time, and approximately 30% of HSA becomes glycated. Circular Dichroism (CD) spectroscopy showed significant changes in the secondary structure of HSA due to glycation. The binding constant (Ka) for AgNPs and HSA with various degrees of glycation was determined with fluorescence quenching titrations. Results indicated a decrease in binding constants for glycated HSA compared to native proteins. These findings contribute to a better understanding of the nature and stability of protein corona formation between glycated protein and silver nanoparticles.
Recommended Citation
Kirk, Megan, "Effect of Glycation on the Binding Interactions of Serum Albumin and Silver Nanoparticles" (2025). Celebrating Scholarship and Creativity Day (2018-). 295.
https://digitalcommons.csbsju.edu/ur_cscday/295
