Luminometric Nanoparticle-Based Assay for High Sensitivity Detection of β-Amyloid Aggregation

Pihlasalo, Sari; Deguchi, Takahiro; Virtamo, Maria; Jacobino, Jenna; Chary, Karthik; López-Picón, Francisco R.; Brunhofer-Bolzer, Gerda; Huttunen, Roope; Fallarero, Adyary; Vuorela, Pia; Härmä, Harri

doi:10.1021/acs.analchem.6b04266

Cited by 12 publications

(11 citation statements)

References 35 publications

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“…A nanoparticle-based probe for the detection of Aβ aggregates was introduced by Pihlasalo and co-workers . Polystyrene nanoparticles were doped with Eu(III) (Figure ), and the particles were mixed with a labeled protein that would receive energy from the particle through luminescence resonance energy transfer (LRET).…”

Section: Materials-based Probes For Sensing Amyloid Aggregatesmentioning

confidence: 99%

“…A nanoparticle-based probe for the detection of Aβ aggregates was introduced by Pihlasalo and co-workers. 124 Polystyrene nanoparticles were doped with Eu(III) (Figure 19), and the particles were mixed with a labeled protein that would receive energy from the particle through luminescence resonance energy transfer (LRET). In the presence of monomeric Aβ 1−42 , the surface would be mostly covered by monomeric Aβ preventing the labeled protein from approaching the particle (Figure 19, left).…”

Section: Nanoparticlesmentioning

confidence: 99%

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Interrogating Amyloid Aggregates using Fluorescent Probes

Aliyan

Cook

Martí³

2019

Chem. Rev.

215

193

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Amyloids are a broad class of proteins and peptides that can misfold and assemble into long unbranched fibrils with a cross-β conformation. These misfolding and aggregation events are associated with the onset of a variety of human diseases, among them, Alzheimer’s disease, Parkinson’s disease, and Huntington disease. Our understanding of amyloids has been greatly supported by fluorescent molecular probes, such as thioflavin-T, which shows an increase in fluorescence emission upon binding to fibrillar aggregates. Since the first application of thioflavin-T in amyloid studies nearly 30 years ago, many probes have emerged exhibiting a variety of responses to amyloids, such as intensity changes, shifts in fluorescence maxima, and variations in lifetimes, among many others. These probes have shed light on a variety of topics including the kinetics of amyloid aggregation, the effectiveness of amyloid aggregation inhibitors, the elucidation of binding sites in amyloid structures, and the staining of amyloids aggregates in vitro, ex vivo, and in vivo. In this Review, we discuss the design, properties, and application of photoactive probes used to study amyloid aggregation, as well as the challenges faced by current probes and techniques, and the novel approaches that are emerging to address these challenges.

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Section: Materials-based Probes For Sensing Amyloid Aggregatesmentioning

confidence: 99%

Section: Nanoparticlesmentioning

confidence: 99%

Interrogating Amyloid Aggregates using Fluorescent Probes

Aliyan

Cook

Martí³

2019

Chem. Rev.

215

193

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“…Alzheimer’s disease (AD) was associated with the loss of neurons and caused memory damage, and language and physical disorders, , which have forced a huge economic burden on human health. − β-Amyloid (Aβ), which majorly includes Aβ peptide of 39–43 amino acids, has been broadly considered as an important biomarker and therapeutic target for AD. − The recent research studies have demonstrated clearly that the regulation of the Aβ aggregation is acknowledged as a potential and promising therapeutic strategy for AD. − …”

Section: Introductionmentioning

confidence: 99%

“…Presently, a variety of aggregation inhibitors, such as small molecules, − antibodies, , proteins (peptides), − aptamers, − polymers, − and nanomaterials, − were discovered for regulating the Aβ aggregation. Especially, the aptamer was considered as a promising inhibitor (Table S1).…”

Section: Introductionmentioning

confidence: 99%

Development of DNA Aptamer as a β-Amyloid Aggregation Inhibitor

Zheng

Wang

et al. 2020

ACS Appl. Bio Mater.

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Developing a strategy of modulating β-amyloid (Aβ) aggregation with low cost, easy synthesis, high efficiency, and biosafety is significant and a challenge for Alzheimer’s disease (AD) therapy. Herein, DNA aptamer (Aβ-Apt) against Aβ42 obtained by in vitro selection was developed as a potent inhibitor of Aβ42 aggregation for the first time. Indeed, the Aβ42 monomer fibrillation was inhibited completely by Aβ-Apt. Notably, the inhibition effect of Aβ-Apt on the Aβ42 oligomer aggregation was more obvious than that on the Aβ42 monomer aggregation. It was presumed that the distinguishing effect may be attributed to different binding behaviors of Aβ-Apt with Aβ42 monomer and Aβ42 oligomer. Surface plasmon resonance analysis demonstrated that Aβ-Apt specifically recognized Aβ42 monomer and Aβ42 oligomer. Furthermore, the binding affinity of Aβ-Apt with Aβ42 oligomer was larger than that of Aβ-Apt with Aβ42 monomer. This work provided a promising platform with high efficiency for manipulating Aβ aggregation.

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“…Meanwhile, researchers have also made many efforts to develop amyloid aggregation inhibitors in order to promote the therapy of AD. They have discovered kinds of Aβ aggregation-regulated molecules and nanomaterials by exploring the interaction between amyloid and antibodies 33 - 38 , peptides 39 - 44 , small molecules 45 - 51 , aptamers 52 - 56 , polymers 57 - 59 , as well as nanomaterials 60 - 63 . Most of these inhibitors can regulate the aggregation process of Aβ in vitro or in vivo and reduce the cytotoxicity caused by Aβ aggregates to a certain extent, providing a valuable treatment strategy for delaying AD progression.…”

Section: Introductionmentioning

confidence: 99%

Advances in aptamers against Aβ and applications in Aβ detection and regulation for Alzheimer's disease

Zheng¹,

Zhang²,

Zhao³

et al. 2022

Theranostics

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Alzheimer's disease (AD) is an irreversible neurodegenerative disease, causing profound social and economic implications. Early diagnosis and treatment of AD have faced great challenges due to the slow and hidden onset. β-amyloid (Aβ) protein has been considered an important biomarker and therapeutic target for AD. Therefore, non-invasive, simple, rapid and real-time detection methods for AD biomarkers are particularly favored. With the development of Aβ aptamers, the specific recognition between aptamers and Aβ plays a significant role in AD theranostics. On the one hand, aptamers are applied to construct biosensors for Aβ detection, which provides possibilities for early diagnosis of AD. On the other hand, aptamers are used for regulating Aβ aggregation process, which provides potential strategies for AD treatment. Many excellent reviews have summarized aptamers for neurodegenerative diseases or biosensors using specific recognition probes for Aβ detection applications in AD. In this review, we highlight the crucial role of the design, classification and applications of aptamers on Aβ detection as well as inhibition of Aβ aggregation for AD.

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Luminometric Nanoparticle-Based Assay for High Sensitivity Detection of β-Amyloid Aggregation

Cited by 12 publications

References 35 publications

Interrogating Amyloid Aggregates using Fluorescent Probes

Interrogating Amyloid Aggregates using Fluorescent Probes

Development of DNA Aptamer as a β-Amyloid Aggregation Inhibitor

Advances in aptamers against Aβ and applications in Aβ detection and regulation for Alzheimer's disease

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