Confirming and Characterizing the Potential Interaction Between Serum Albumin and the Insulin-Resistance Protein Fetuin-A

Author

• John A. Mullins, Stephen F Austin State UniversityFollow

Date of Award

Summer 8-6-2026

Degree Type

Thesis

Degree Name

Master of Science - Natural Sciences

Department

Chemistry and Biochemistry

First Advisor

Dr. Odutayo Odunuga

Abstract

Serum albumin is a water-soluble, globular protein found in all vertebrates. It is the most abundant plasma protein, responsible for maintaining oncotic pressure, regulating blood pH, and transporting numerous drugs, fatty acids, and proteins. Bioinformatic analysis revealed potential interactions with another plasma protein, Fetuin-A. Fetuin-A is a multifunctional glycoprotein implicated in blood sugar regulation and type II diabetes. To date, their direct physical interaction has not been experimentally probed. The present study confirmed and characterized this interaction by using pull-down assays and surface plasmon resonance (SPR) spectroscopy. Pull-down assays revealed a concentration-dependent binding between the two proteins. Kinetic analysis of the SPR sensorgrams using a simple 1:1 binding interaction model, alongside steady-state affinity analysis, yielded estimated K_D values within the nanomolar range, indicating a high-affinity interaction. These findings provide new evidence for their direct physical interaction and offer a foundation for future studies on their role in blood sugar regulation.

Repository Citation

Mullins, John A., "Confirming and Characterizing the Potential Interaction Between Serum Albumin and the Insulin-Resistance Protein Fetuin-A" (2026). Electronic Theses and Dissertations. 677.
https://scholarworks.sfasu.edu/etds/677

Creative Commons License

This work is licensed under a Creative Commons Attribution-Noncommercial-No Derivative Works 4.0 License.