A rapid, sensitive and specific detection of aggregated α-Synuclein by a liposome-immobilized cantilever sensor

Parkinson's disease (PD) is characterized by dopaminergic cell loss and the formation of Lewy bodies, of which the main component is aggregated and fibrillized alpha-synuclein (aSyn). Recent studies suggested that ultra-trace amounts of aSyn aggregates are also present in biofluid specimens, an...

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Published in:IEEE sensors journal 2023-06, Vol.23 (12), p.1-1
Main Authors: Kobayashi, Ryoko, Kamitani, Kotaro, Sawamura, Masanori, Yamakado, Hodaka, Takahashi, Ryosuke, Sohgawa, Masayuki, Noda, Minoru
Format: Article
Language:English
Subjects:
Aggregates
Biomarkers
cantilever sensor
Diseases
Lag time
Lipids
liposome
Liposomes
Parkinson disease
Parkinson's disease
prion-lipid interaction
Proteins
self-templating assembly
Sensitivity enhancement
Sensor phenomena and characterization
Sensors
Surface stress
Temperature sensors
α-synuclein
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Kamitani, Kotaro
Sawamura, Masanori
Yamakado, Hodaka
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Sohgawa, Masayuki
Noda, Minoru
description Parkinson's disease (PD) is characterized by dopaminergic cell loss and the formation of Lewy bodies, of which the main component is aggregated and fibrillized alpha-synuclein (aSyn). Recent studies suggested that ultra-trace amounts of aSyn aggregates are also present in biofluid specimens, and they can serve as a biomarker for PD. Because aSyn has been shown to possess a prion-like property, we attempted to enhance the sensitivity and specificity of a cantilever microsensor to detect aSyn aggregates by exploiting the properties of self-templating assembly and lipid interaction on the surface of liposome-immobilized cantilever sensor. We found that the liposome-immobilized cantilever sensor was able to successfully detect aSyn fibrils at a very low concentration (100 pg/ml), and the addition of aSyn monomers, which were converted into fibrils in the presence of aSyn aggregates and further acted as a template for fibrillization, lowered the detection limit to 10 pg/ml. The sensitivity of this cantilever sensor was comparable to or slightly superior to that of enzyme-linked immunosorbent assay (ELISA). Moreover, the lag time for the detection of aSyn fibrils has been significantly reduced to 100-120 minutes, compared to the tens of hours needed in conventional ELISA, Real-Time Quaking-Induced Conversion (RT-QuIC) and Protein Misfolding Cyclic Amplification (PMCA) assays. Finally, preliminary measurements of aSyn aggregates showed the possibilities of discriminating serum from PD and non-PD patients. The liposome-immobilized cantilever sensor could serve as a promising tool for the early or preclinical diagnosis of PD.
doi_str_mv 10.1109/JSEN.2023.3272659
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source IEEE Electronic Library (IEL) Journals
subjects Aggregates
Biomarkers
cantilever sensor
Diseases
Lag time
Lipids
liposome
Liposomes
Parkinson disease
Parkinson's disease
prion-lipid interaction
Proteins
self-templating assembly
Sensitivity enhancement
Sensor phenomena and characterization
Sensors
Surface stress
Temperature sensors
α-synuclein
title A rapid, sensitive and specific detection of aggregated α-Synuclein by a liposome-immobilized cantilever sensor
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