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Aβ plaque-selective NIR fluorescence probe to differentiate Alzheimer's disease from tauopathies
KTH, School of Biotechnology (BIO), Theoretical Chemistry and Biology.ORCID iD: 0000-0003-0185-5724
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2017 (English)In: Biosensors & bioelectronics, ISSN 0956-5663, E-ISSN 1873-4235, Vol. 98, p. 54-61Article in journal (Refereed) Published
Abstract [en]

Selective detection and staining of toxic amyloid plaques, a potential biomarker present in the Alzheimer's disease (AD) brain is crucial for both clinical diagnosis and monitoring AD disease progression. Herein, we report a coumarin-quinoline (CQ) conjugate-based turn-on near-infrared (NIR) fluorescence probe for specific detection of β-amyloid (Aβ) aggregates. CQ probe is highly sensitive and exhibits ~100-fold fluorescence enhancement in vitro upon binding Aβ aggregates with enhanced quantum yield. Furthermore, the probe has ~10-fold higher binding affinity towards Aβ aggregates (86 nM) compared to commonly used Thioflavin T. Most importantly, CQ probe displays unambiguous selectivity towards Aβ aggregates compared to other toxic protein aggregates such as tau, α-synuclein (α-Syn) and islet amyloid polypeptide (IAPP). In addition, CQ is nontoxic to neuronal cells and shows significant blood brain barrier permeability. Remarkably, CQ stains Aβ plaques in human brain tissue over co-existing tau aggregates and neurofibrillary tangles (NFTs), which are associated in AD and tauopathies. This is a highly desirable attribute to distinguish AD from tau pathology and mixed dementia.

Place, publisher, year, edition, pages
Elsevier Ltd , 2017. Vol. 98, p. 54-61
Keywords [en]
Alzheimer's disease, Mixed dementia, Neurofibrillary tangles (NFTs), NIR fluorescence probes, Selective detection of Aβ42 plaques, Tauopathies, Aggregates, Binding energy, Bins, Brain, Diagnosis, Fluorescence, Glycoproteins, Infrared devices, Probes, Neurofibrillary tangles, NIR fluorescences, Selective detection, Neurodegenerative diseases, alpha synuclein, amylin, amyloid beta protein, coumarin, quinoline, tau protein, thioflavine, Alzheimer disease, amyloid plaque, analytic method, Article, binding affinity, binding site, blood brain barrier, brain tissue, calculation, controlled study, fluorescence analysis, fluorescence resonance energy transfer, human, human tissue, in vitro study, molecular docking, molecular weight, near infrared fluorescence probe, neurofibrillary tangle, physical chemistry, protein aggregation, protein folding, quantum yield, tauopathy
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Clinical Laboratory Medicine
Identifiers
URN: urn:nbn:se:kth:diva-218607DOI: 10.1016/j.bios.2017.06.030Scopus ID: 2-s2.0-85021075724OAI: oai:DiVA.org:kth-218607DiVA, id: diva2:1161470
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QC 20171130

Available from: 2017-11-30 Created: 2017-11-30 Last updated: 2017-11-30Bibliographically approved

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Natarajan Arul, Murugan

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