Current Search: ("ddu@fau.edu") (x)
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Title
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Gold Nanoparticles as a Probe for Amyloid-β Oligomer and Amyloid Formation.
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Creator
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Esmail A. Elbassal, Clifford Morris, Thomas W. Kent, Thomas W. Kent, Bimlesh Ojha, Ewa P. Wojcikiewicz, Deguo Du
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Abstract/Description
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The process of amyloid-β (Aβ) amyloid formation is pathologically linked to Alzheimer’s disease (AD). The identification of Aβ amyloids and intermediates that are crucial players in the pathology of AD is critical for exploring the underlying mechanism of Aβ aggregation and the diagnosis of the disease. Herein, we performed a gold nanoparticle (AuNP)-based study to detect the formation of Aβ amyloid fibrils and oligomers. Our results demonstrate that the intensity of the surface plasmon...
Show moreThe process of amyloid-β (Aβ) amyloid formation is pathologically linked to Alzheimer’s disease (AD). The identification of Aβ amyloids and intermediates that are crucial players in the pathology of AD is critical for exploring the underlying mechanism of Aβ aggregation and the diagnosis of the disease. Herein, we performed a gold nanoparticle (AuNP)-based study to detect the formation of Aβ amyloid fibrils and oligomers. Our results demonstrate that the intensity of the surface plasmon resonance (SPR) absorption band of the AuNPs is sensitive to the quantity of Aβ40 amyloids. This allows the SPR assay to be used for detection and semi-quantification of Aβ40 amyloids, and characterization of the kinetics of Aβ amyloid formation. Furthermore, our study demonstrates that the SPR band intensity of the AuNPs is sensitive to the presence of oligomers of both Aβ40 and an Aβ40 mutant, which forms more stable oligomers. The kinetics of the stable oligomer formation of the Aβ40 mutant can also be monitored following the SPR band intensity change of AuNPs. Our results indicate that this nanoparticle based method can be used for mechanistic studies of early protein self-assembly and fibrillogenesis.
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Date Issued
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2017
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PURL
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http://purl.flvc.org/fau/fd/FAUIR000499
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Format
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Document (PDF)
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Title
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A Kinetic Aggregation Assay Enabling Selective and Sensitive Aβ Amyloid Quantification in Cells and Tissues.
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Creator
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Deguo Du, Amber N. Murray, Ehud Cohen, Hyun-Eui Kim, Ryan Simkovsky, Andrew Dillin, Jeffery W. Kelly
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Abstract/Description
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The process of amyloid-β (Aβ) fibril formation is genetically and pathologically linked to Alzheimer's disease (AD). Thus, a selective and sensitive method for the quantification of Aβ amyloid fibrils in complex biological samples enables a variety of hypotheses to be tested. Herein we report the basis for a quantitative in vitro kinetic aggregation assay that detects seeding competent Aβ aggregates in mammalian cell culture media, in Caenorhabditis elegans lysate and in mouse brain...
Show moreThe process of amyloid-β (Aβ) fibril formation is genetically and pathologically linked to Alzheimer's disease (AD). Thus, a selective and sensitive method for the quantification of Aβ amyloid fibrils in complex biological samples enables a variety of hypotheses to be tested. Herein we report the basis for a quantitative in vitro kinetic aggregation assay that detects seeding competent Aβ aggregates in mammalian cell culture media, in Caenorhabditis elegans lysate and in mouse brain homogenate. Sonicated, proteinase K treated Aβ-fibril-containing tissue homogenates or cell culture media were added to an initially monomeric Aβ1–40 reporter peptide to seed an in vitro nucleated aggregation reaction. The reduction in the half time (t50) of the amyloid growth phase is proportional to the quantity of seeding-competent Aβ aggregates present in the biological sample. An ion exchange resin amyloid isolation strategy from complex biological samples is demonstrated as an alternative to improve the sensitivity and linearity of the kinetic aggregation assay.
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Date Issued
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2011
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PURL
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http://purl.flvc.org/fau/fd/FAUIR000498
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Format
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Document (PDF)
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Title
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Temporal requirements of insulin/IGF‐1 signaling for proteotoxicity protection.
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Creator
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Cohen, Ehud, Du, Deguo, Joyce, Derek, Kapernick, Erik A., Volovik, Yuli, Kelly, Jeffery W., Dillin, Andrew
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Date Issued
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2010-04-16
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PURL
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http://purl.flvc.org/fau/flvc_fau_islandoraimporter_10.1111_j.1474-9726.2009.00541.x_1648044589
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Format
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Document (PDF)
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Title
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Evaluating β-turn mimics as β-sheet folding nucleators.
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Creator
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Fuller, Amelia A., Du, Deguo, Liu, Feng, Davoren, Jennifer E., Bhabha, Gira, Kroon, Gerard, Case, David A., Dyson, H. Jane, Powers, Evan T., Wipf, Peter, Gruebele, Martin, Kelly, Jeffery W.
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Date Issued
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2009-07-07
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PURL
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http://purl.flvc.org/fau/flvc_fau_islandoraimporter_10.1073_pnas.0813012106_1648043559
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Format
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Document (PDF)
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Title
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An experimental survey of the transition between two-state and downhill protein folding scenarios.
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Creator
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Liu, Feng, Du, Deguo, Fuller, Amelia A., Davoren, Jennifer E., Wipf, Peter, Kelly, Jeffery W., Gruebele, Martin
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Date Issued
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2008-02-19
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PURL
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http://purl.flvc.org/fau/flvc_fau_islandoraimporter_10.1073_pnas.0711908105_1647975037
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Format
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Document (PDF)
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Title
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Trp zipper folding kinetics by molecular dynamics and temperature-jump spectroscopy.
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Creator
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Snow, Christopher D., Qiu, Linlin, Du, Deguo, Gai, Feng, Hagen, Stephen J., Pande, Vijay S.
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Date Issued
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2004-03-23
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PURL
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http://purl.flvc.org/fau/flvc_fau_islandoraimporter_10.1073_pnas.0305260101_1647885925
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Format
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Document (PDF)
