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The impact of modified polystyrene on lysozyme fibrillation studied by surface-enhanced Raman spectroscopy (SERS)
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Researchers used surface-enhanced Raman spectroscopy and FTIR to investigate how surface chemical modifications of polystyrene nanoplastics (unmodified, carboxyl-modified, and amino-modified) affect lysozyme fibrillation. Amino-modified PS promoted fibrillation at 10 microg/mL comparable to unmodified and carboxyl-modified PS at 50 microg/mL, acting primarily through enhancement of primary nucleation, with a distinctive SERS signal confirming interaction between amino groups and tryptophan/tyrosine residues of the protein.
Nanoplastics could modulate the fibrillation of amyloid proteins. However, many chemical functional groups are adsorbed to change the interfacial chemistry of nanoplastics in the real world. Herein, this study aimed to investigate the effects of polystyrene (PS), carboxyl modified PS (PS-COOH), and amino modified PS (PS-NH) on the fibrillation of hen egg-white lysozyme (HEWL). Due to the differences in the interfacial chemistry, concentration was considered an essential factor. PS-NH (10 μg/mL) could promote the fibrillation of HEWL similar to PS (50 μg/mL) and PS-COOH (50 μg/mL). Moreover, promoting the primary nucleation step of amyloid fibril formation was the primary reason. The differences in spatial conformation of HEWL were characterized by Fourier transform-infrared spectroscopy and surface enhanced Raman spectroscopy (SERS). Strikingly, a particular signal of SERS of HEWL incubated with PS-NH at 1610 cm was found due to the interaction between amino group of PS-NH and tryptophan (or tyrosine) of HEWL. Therefore, a new perspective was provided to understand the regulation of interfacial chemistry of nanoplastics on the fibrillation of amyloid proteins. Additionally, this study suggested that SERS could be a powerful method to investigate the interactions between proteins and nanoparticles.
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Submicron polystyrene particles (400 nm) promoted the formation of amyloid fibrils in hen egg-white lysozyme by adsorbing to the protein surface and altering its folding dynamics, an effect mediated through the protein corona that forms on nanoplastic surfaces. The findings raise concern that nanoplastics could seed or accelerate amyloid aggregation processes relevant to neurodegenerative diseases.
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