Nonenzymatic glycation of human serum albumin affects its structure, properties, and binding interactions with silver nanoparticles

Authors

• Monica Fairchild, College of Saint Benedict and Saint John's University
• Megan Kirk, College of Saint Benedict and Saint John's University
• Collin Kray, College of Saint Benedict and Saint John's University

Document Type

Poster

Publication Date

4-30-2026

Disciplines

Biochemistry, Biophysics, and Structural Biology

Advisor

Md Fazal

Abstract

Most nanoparticles (1-100 nm), upon contact with proteins, form a “protein corona” which can alter the structure and function of proteins. Human serum albumin (HSA) is the most abundant protein in blood plasma and acts as a major transport protein for numerous endogenous and exogenous compounds. In healthy individuals, 1-10% HSA is found in a glycated state, but significantly higher levels of glycated HSA (30% or more) are found in Diabetic individuals. This project investigates the effects of glycation on the structure, enzymatic activity, and antioxidant capacity of HSA and its binding interactions with silver nanoparticles (AgNPs) using a variety of spectroscopic techniques. Circular Dichroism (CD) spectroscopy indicated a significant change in the secondary structures of HSA due to glycation. The glycated HSA showed a significant decrease in the enzymatic activity and antioxidant capacity of the protein. The fluorescence quenching experiments demonstrated a lower binding affinity of glycated HSA to silver nanoparticles compared to the native protein. These results contribute to a better understanding of the effects of nonenzymatic glycation on the structure and function of proteins in the human body.

Recommended Citation

Fairchild, Monica; Kirk, Megan; and Kray, Collin, "Nonenzymatic glycation of human serum albumin affects its structure, properties, and binding interactions with silver nanoparticles" (2026). Celebrating Scholarship and Creativity Day (2018-). 371.
https://digitalcommons.csbsju.edu/ur_cscday/371