Applications of nanotechnology as drugs or in diagnostics developments can be complicated by biomolecular interactions and physiological conditions that vary across individuals. Among the biomolecules that mediate nanoparticle transformations and fate are a population of proteins that adsorb to the nanoparticle surface, known as the protein corona. Variations in the protein corona depend on the biophysical features of the solution and nanoparticles, as well as the population of proteins. Recent results have even demonstrated that the protein corona varies with a patient’s disease states. In addition to alterations in the protein population, disease states alter protein post- translational modifications (PTMs). Despite a decade of research in the protein corona, the role of PTMs in mediating protein interactions with nanomaterials remain poorly understood. Here we present data on how a common PTM, glycation, alters nanoparticle interactions of the most abundant blood protein, human serum albumin (HSA). The effects of glycation on HSA interactions with silver nanoparticles have been evaluated with fluorescence quenching experiments to gain insight into changes in binding affinity. In addition, we evaluated changes to the protein and particle upon interactions. Protein structural changes were monitored using circular dichroism spectroscopy, while nanoparticle transformations were monitored to assess particle agglomeration, surface charge, and dissolution. The results provide insight into how protein glycation alters protein corona formation. This dataset serves as the first step to interrogating the role of PTMs in altering protein corona formation.

Glycation of human serum albumin alters nanoparticle-protein interactions

2019 Fall National Meeting

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