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Abstract 1036 A Biochemical Investigation on the Structural Integrity of Bovine Serum Albumin During Exposure to Plastic Particles
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This biochemical study investigated how microplastics and nanoplastics at varying concentrations affect the structural integrity of bovine serum albumin, finding that plastic particles induce conformational changes in the protein that may indicate broader impacts on biological macromolecules.
Plastic pollution is a growing global health problem that has broad research implications. This project explored the effects of microplastics (MPs, 5mm – 1μm) and nanoplastics (NPs, 999nm – 1nm) on the overall molecular structure of bovine serum albumin (BSA), a transporter of fatty acids and common in vitro protein stabilizer. As plastic breaks down in nature due to a multitude of mechanical and chemical forces, it can become small enough to pass through the blood-brain barrier and interact with blood-borne proteins. Within this study, BSA serves as a model for determining the potential extent of this interaction, which was measured using circular dichroism (CD) spectroscopy, microscopy, and preliminary protein docking computational calculations. CD spectra revealed that BSA underwent significant global structural changes after exposure to polypropylene (PP) MPs and NPs at 20˚C. CD data obtained during thermal denaturation assays revealed that while the melting temperature (Tm) of BSA decreases from 61˚C to 60˚C after exposure to plastic particles, the thermodynamics of unfolding were notably different which again indicated notable structural changes. Secondary structural analysis of BSA from CD spectra revealed that before exposure to MPs and NPs, BSA was shown to have 55.5% alpha helices, 17.4% beta sheets, 11.9% beta turns, and 15.2% random coiling. After exposure to MPs and NPs, those values changed to 57.9%, 13.6%, 15%, and 13.5% respectively. Comparing those values to docking data revealed that the potential binding pockets for PP altered the secondary and tertiary structures as well. The proposed binding affinities for PP in BSA revealed that it binds strongly enough to the protein for its natural efficiency to be impeded due to decreased availability to transport. This work was financially supported by St. Mary's College of Maryland, NSF MRI grant #1919581, and the Sherman Fairchild Foundation SEP grant.
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