Quench-type electrochemiluminescence immunosensor for detection of amyloid β-protein based on resonance energy transfer from luminol@SnS-Pd to Cu doped WO nanoparticles.

08:00 EDT 19th March 2019 | BioPortfolio

Summary of "Quench-type electrochemiluminescence immunosensor for detection of amyloid β-protein based on resonance energy transfer from luminol@SnS-Pd to Cu doped WO nanoparticles."

A highly efficient quench-type electrochemiluminescence (ECL) immunosensor was proposed for the trace detection of amyloid β-protein (Aβ). In this work, tin disulfide nanoflowers (SnS NFs) with large specific surface area, favorable catalytic property and chemical stability were prepared and used as substrate material. Taking advantage of the excellent catalytic ability and biocompatibility, palladium nanoparticles (Pd NPs) were in situ reduced on SnS NFs to obtain SnS-Pd. Moreover it could combine with large amounts of luminol and achieve a strong ECL signal output. In addition, copper doped mesoporous tungsten trioxide (Cu:WO) nanoparticles were selected to quench ECL emission of luminol@SnS-Pd via resonance energy transfer, where luminol@SnS-Pd was the donor and Cu:WO was the acceptor. On this basis, a quench-type ECL immunosensor was constructed for detection of Aβ. Under optimum conditions, the fabricated ECL immunosensor showed sensitive response to Aβ concentration from 0.1 pg/mL to 50 ng/mL with a low detection limit of 5.4 fg/mL (S/N = 3). It is expected to be a promising analytical tool for the sensitive detection of Aβ and other biomarkers with high specificity, good reproducibility and long-term stability.


Journal Details

This article was published in the following journal.

Name: Biosensors & bioelectronics
ISSN: 1873-4235
Pages: 192-198


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Medical and Biotech [MESH] Definitions

A type of extracellularly deposited substance composed of an amyloid protein and additional components including HEPARAN SULFATE PROTEOGLYCAN; LAMININ; COLLAGEN TYPE IV; SERUM AMYLOID P-COMPONENT; and APOLIPOPROTEINS E which together form characteristic amyloid fibrils. The core of amyloid fibrils is formed by the stacking of overlapping beta-pleated sheet domains of the amyloid protein. There are many different amyloid proteins that have been found forming the core of the fibrils in vivo. However, amyloid can be formed from any protein that exposes beta-pleated strand conformations during unfolding or refolding. A common characteristic of amyloid is the ability to bind such dyes as CONGO RED and thioflavine.

Endopeptidases that are specific for AMYLOID PROTEIN PRECURSOR. Three secretase subtypes referred to as alpha, beta, and gamma have been identified based upon the region of amyloid protein precursor they cleave.

An ACUTE PHASE REACTION protein present in low concentrations in normal sera, but found at higher concentrations in sera of older persons and in patients with AMYLOIDOSIS. It is the circulating precusor of amyloid A protein, which is found deposited in AA type AMYLOID FIBRILS.

Proteins that form the core of amyloid fibrils. For example, the core of amyloid A is formed from amyloid A protein, also known as serum amyloid A protein or SAA protein.

A precursor to the AMYLOID BETA-PROTEIN (beta/A4). Alterations in the expression of the amyloid beta-protein precursor (ABPP) gene, located on chromosome 21, plays a role in the development of the neuropathology common to both ALZHEIMER DISEASE and DOWN SYNDROME. ABPP is associated with the extensive extracellular matrix secreted by neuronal cells. Upon cleavage, this precursor produces three proteins of varying amino acid lengths: 695, 751, and 770. The beta/A4 (695 amino acids) or beta-amyloid protein is the principal component of the extracellular amyloid in senile plaques found in ALZHEIMER DISEASE; DOWN SYNDROME and, to a limited extent, in normal aging.

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