We can't find the internet
Attempting to reconnect
Something went wrong!
Hang in there while we get back on track
PathologicalFolding of α‑Synuclein onPolystyrene Nanoplastic Revealed by Sum Frequency Scattering and 2DInfrared Spectroscopy
AI summary Read the abstract
Using sum frequency scattering and 2D infrared spectroscopy, researchers characterized the molecular structure of alpha-synuclein adsorbed on polystyrene nanoplastics, finding that the plastic surface induced pathological protein folding patterns similar to those seen in Parkinson's disease.
The impact of micro- and nanoplastics (MNPs) on human health is a growing field of research. Reports that MNPs can breach the blood-brain barrier and accumulate inside the brain have raised concerns over their possible involvement in the development of neurogenerative diseases. The aggregation of the abundant neuronal protein α-synuclein (α-syn) is pertinent to almost 50 neurological diseases including Parkinson’s disease (PD). The role of nanoplastics in the formation of toxic aggregates is unclear and has been shown to depend strongly on the type of plastics. Here we report the molecular structure and orientation of human α-syn adsorbed on polystyrene NPs using interface-specific sum frequency scattering (SFS) and structure-sensitive two-dimensional infrared (2D IR) spectroscopy. The SFS experimental data were compared with the calculated spectra of several thousands of α-syn conformations generated from molecular dynamics simulations. The SFS results reveal that α-syn folds on polystyrene nanoplastics, adopting a partly helical structure with the N-terminus and nonamyloid component regions directly bound on the polystyrene nanosurface, while the C terminus protrudes away from the polystyrene interface. 2D IR results suggest that the entire α-syn corona comprises of partly aggregated α-syn structures, built of an ordered core enclosed with flexible dynamic regions. The data shed light on the mechanism by which α-syn folds and forms aggregates at the plastic particle surfaces, a link that has been missing in understanding the role of nanoplastic in the pathogenesis of PD and related neurodegenerative diseases.
More Papers Like This
Pathological Folding of α-Synuclein on Polystyrene Nanoplastic Revealed by Sum Frequency Scattering and 2D Infrared Spectroscopy
AI summary Read the abstract
Researchers used advanced spectroscopy techniques to study how the neuronal protein alpha-synuclein interacts with polystyrene nanoplastics at the molecular level. The study found that nanoplastics can induce pathological folding patterns in alpha-synuclein, which is relevant to understanding potential links between plastic particle exposure and neurodegenerative conditions like Parkinson's disease.
Insights into the Binding Interactions between Microplastics and Human α-Synuclein Protein by Multispectroscopic Investigations and Amyloidogenic Oligomer Formation
AI summary Read the abstract
Researchers found that common microplastics -- especially polystyrene -- can bind to alpha-synuclein, a brain protein whose clumping is a hallmark of Parkinson's disease. The microplastics altered the protein's structure and promoted the formation of toxic clumps called amyloidogenic oligomers. This suggests that microplastic exposure could potentially accelerate the protein misfolding process linked to Parkinson's and other neurodegenerative diseases.
Protein aggregation, hydrophobicity and neurodegenerative disease
AI summary Read the abstract
This doctoral thesis on protein aggregation and neurodegenerative disease includes an important finding relevant to microplastics: nanoscale PET plastic particles were shown to accelerate the formation of amyloid fibrils from alpha-synuclein, a protein central to Parkinson's disease. This raises the concern that everyday nanoplastic exposure could contribute to the onset or progression of neurodegenerative conditions.
Nanoplastic Stimulates the Amyloidogenesis of Parkinson's Alpha‐Synuclein NACore
AI summary Read the abstract
This study found that nanoplastic particles can accelerate the clumping of a protein called alpha-synuclein, which is linked to Parkinson's disease. Using advanced mass spectrometry, researchers showed that nanoplastics sped up the formation of harmful protein clusters and increased their toxicity to brain cells. The findings suggest that nanoplastic exposure could be a factor worth investigating in neurodegenerative disease research.
Exploring the Interaction of Human α-Synuclein with Polyethylene Nanoplastics: Insights from Computational Modeling and Experimental Corroboration
AI summary Read the abstract
Researchers used computer simulations and lab experiments to study how polyethylene nanoplastics interact with alpha-synuclein, a brain protein linked to neurodegenerative conditions. They found that nanoplastics caused the protein to change its shape and form a compact structure that interacts more strongly with itself, potentially promoting clumping. The study suggests a possible mechanism by which nanoplastics could influence protein behavior in the brain, though the health implications remain to be determined.
Research digests by email
When a large batch of papers lands in the Atlas, we read through it and send a short write-up of what stood out.