A highly sensitive electrochemical impedance sensor for amyloid beta oligomer (AβO) was fabricated using a cellular prion protein (PrP) bioreceptor linked with poly(thiophene-3-acetic acid) transducer. An additional thin layer of poly(3,4-ethylene dioxythiophene) embedded with gold nanoparticles was employed to provide high electrical conductivity and a large surface area. The sensing performace was investigated in terms of sensitivity and detection range. The fabricated sensor exhibited extremely low detection limit at a subfemtomolar level with a wide detection range from 10 to 10 nM and its utility was established in mice infected with Alzheimer's disease (AD). The developed AβO sensor could be utilized for early diagnosis of AD.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1021/acs.analchem.9b02266 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Bioinformatics Analysis Reveals Microrchidia Family Genes as the Prognostic and Therapeutic Markers for Colorectal Cancer.
Endocr Metab Immune Disord Drug Targets
January 2025
Department of Laboratory Medicine, Taizhou First People's Hospital, Huangyan Hospital of Wenzhou Medical University, Taizhou, Zhejiang, China.
Aim: The aim of this study is to examine the role of the microrchidia (MORC) family, a group of chromatin remodeling proteins, as the therapeutic and prognostic markers for colorectal cancer (CRC).
Background: MORC protein family genes are a highly conserved nucleoprotein superfamily whose members share a common domain but have distinct biological functions. Previous studies have analyzed the roles of MORCs as epigenetic regulators and chromatin remodulators; however, the involvement of MORCs in the development and pathogenesis of CRC was less examined.
In vivo base editing extends lifespan of a humanized mouse model of prion disease.
Nat Med
January 2025
Merkin Institute of Transformative Technologies in Healthcare, Broad Institute of MIT and Harvard, Cambridge, MA, USA.
Prion disease is a fatal neurodegenerative disease caused by the misfolding of prion protein (PrP) encoded by the PRNP gene. While there is currently no cure for the disease, depleting PrP in the brain is an established strategy to prevent or stall templated misfolding of PrP. Here we developed in vivo cytosine and adenine base strategies delivered by adeno-associated viruses to permanently modify the PRNP locus to achieve PrP knockdown in the mouse brain.
View Article and Find Full Text PDFCRISPR/Cas9-editing of PRNP in Alpine goats.
Vet Res
January 2025
UVSQ, INRAE, BREED, Université Paris-Saclay, 78350, Jouy-en-Josas, France.
Misfolding of the cellular PrP (PrP) protein causes prion disease, leading to neurodegenerative disorders in numerous mammalian species, including goats. A lack of PrP induces complete resistance to prion disease. The aim of this work was to engineer Alpine goats carrying knockout (KO) alleles of PRNP, the PrP-encoding gene, using CRISPR/Cas9-ribonucleoproteins and single-stranded donor oligonucleotides.
View Article and Find Full Text PDFTrazodone, dibenzoylmethane and tauroursodeoxycholic acid do not prevent motor dysfunction and neurodegeneration in Marinesco-Sjögren syndrome mice.
PLoS One
January 2025
Department of Neuroscience, Laboratory of Prion Neurobiology, Istituto di Ricerche Farmacologiche Mario Negri IRCCS, Milan, Italy.
There is no cure for Marinesco-Sjögren syndrome (MSS), a genetic multisystem disease linked to loss-of-function mutations in the SIL1 gene, encoding a BiP co-chaperone. Previously, we showed that the PERK kinase inhibitor GSK2606414 delays cerebellar Purkinje cell (PC) degeneration and the onset of ataxia in the woozy mouse model of MSS. However, GSK2606414 is toxic to the pancreas and does not completely rescue the woozy phenotype.
View Article and Find Full Text PDFThe brain interactome of a permissive prion replication substrate.
Neurobiol Dis
January 2025
Tanz Centre for Research in Neurodegenerative Diseases, University of Toronto, Toronto, Ontario, Canada; Department of Biochemistry, University of Toronto, Toronto, Ontario, Canada. Electronic address:
Bank voles are susceptible to prion strains from many different species, yet the molecular mechanisms underlying the ability of bank vole prion protein (BVPrP) to function as a universal prion acceptor remain unclear. Potential differences in molecular environments and protein interaction networks on the cell surface of brain cells may contribute to BVPrP's unusual behavior. To test this hypothesis, we generated knock-in mice that express physiological levels of BVPrP (M109 isoform) and employed mass spectrometry to compare the interactomes of mouse (Mo) PrP and BVPrP following mild in vivo crosslinking of brain tissue.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!