Bovine Serum Albumin Bends Over Backward to Interact with Aged Plastics: A Model for Understanding Protein Attachment to Plastic Debris.
Margaret M Elmer-DixonLiam P FawcettEmma N SorensenMelissa A Maurer-JonesPublished in: Environmental science & technology (2024)
Plastic pollution, a major environmental crisis, has a variety of consequences for various organisms within aquatic systems. Beyond the direct toxicity, plastic pollution has the potential to absorb biological toxins and invasive microbial species. To better understand the capability of environmental plastic debris to adsorb these species, we investigated the binding of the model protein bovine serum albumin (BSA) to polyethylene (PE) films at various stages of photodegradation. Circular dichroism and fluorescence studies revealed that BSA undergoes structural rearrangement to accommodate changes to the polymer's surface characteristics (i.e., crystallinity and oxidation state) that occur as the result of photodegradation. To understand how protein structure may inform docking of whole organisms, we studied biofilm formation of bacteria Shewanella oneidensis on the photodegraded PE. Interestingly, biofilms preferentially formed on the photodegraded PE that correlated with the state of weathering that induced the most significant structural rearrangement of BSA. Taken together, our work suggests that there are optimal physical and chemical properties of photodegraded polymers that predict which plastic debris will carry biochemical or microbial hitchhikers.
Keyphrases
- human health
- biofilm formation
- risk assessment
- protein protein
- candida albicans
- heavy metals
- microbial community
- pseudomonas aeruginosa
- staphylococcus aureus
- binding protein
- public health
- amino acid
- escherichia coli
- health risk assessment
- small molecule
- molecular dynamics simulations
- single molecule
- climate change
- gram negative
- single cell
- multidrug resistant
- high resolution
- transcription factor
- atomic force microscopy
- room temperature
- high speed
- drug induced
- energy transfer