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Structural Stability of Bovine Serum Albumin upon Adsorption to SOMS Measured by FT-IR

Name: Kylie Marie Schmitz
Major: Biochemistry & Molecular Biology
Minor: Mathematics
Advisor: Paul Edmiston; Sara Martin (second reader)

Swellable organically modified silica (SOMS) is a porous material that has been shown to non-specifically adsorb proteins. The goal of this project was to study whether bovine serum albumin (BSA) maintains a folded state upon adsorption to SOMS. FT-IR measurements were taken for a variety of temperatures and concentrations of denaturants. Sequential adsorption experiments revealed that SOMS irreversibly adsorbs >380 mg of BSA per gram of SOMS. Thermal and chemical stability experiments showed that BSA adsorbed to SOMS maintained stability in temperatures up to 99 °C, solutions with up to 50% EtOH-d6, and guanidine HCl solutions with molarity up to 6 M. Overall, SOMS was found to have a protective effect on BSA molecules, preventing them from unfolding in thermal and chemical denaturing conditions. Future work should further explore how proteins adsorb to SOMS and the limits of stability for adsorbed proteins. There is also an opportunity for further investigation into enzymatic activity for adsorbed biomolecules. Enzyme immobilization and other aspects of protein adsorption have many applications in environmental and medical fields.

 

Posted in Comments Enabled, Independent Study, Symposium 2023 on April 14, 2023.


8 responses to “Structural Stability of Bovine Serum Albumin upon Adsorption to SOMS Measured by FT-IR”

  1. . says:

    What motivated you to research about this topic?

  2. Kylie Schmitz says:

    I am fascinated by tissue engineering and the way our bodies respond to various implantable materials. In order for an engineered material to be safe in medical applications, it must not cause any harm to your body. This project allowed me to understand the way biomolecules interact with surfaces in different environments, which provided a great foundation for further education in biomedical engineering.

  3. Anna Norby says:

    Kylie you are too smart!

    What were some challenges you ran into throughout your study?

  4. Torence says:

    Great work!! Were there any surprising results or outcomes during the course of your research?

  5. Kylie Schmitz says:

    Thanks Anna! The main challenges that I ran into involved finding the best ways to take measurements in each condition. Some materials and solvents raised issues with the machine being used and the region of the spectrum that I was analyzing. I overcame these issues by filtering all of my samples and rinsing them with solvents that would not overlap with the data I was interested in.

  6. Kylie Schmitz says:

    Thank you, Torence! I was very surprised by the stability of BSA in such intense conditions. It amazed me that a protein could be so thoroughly protected by simply adsorbing to a solid surface. These findings make me wonder which types of interactions are occurring and why they are so favorable.

  7. George says:

    What was the most difficult thing you had to go through to complete this project?

  8. Kylie Schmitz says:

    Thanks for your question, George! I think the most difficult part of this project was managing my time so that I could complete all my lab work while staying on track with the timing of my experiments. It was also difficult to organize my thoughts in the paper since I am most interested in the medical applications of this project, but also wanted to explain the other applications of protein immobilization.

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