Literature DB >> 23173070

Facile methodology for monitoring amyloid-β fibrillization.

Nathan P Cook1, Angel A Martí.   

Abstract

Amyloid-β (Aβ) is a peptide fragment that is prone to aggregate into large fibrils under physiological conditions. Many techniques have been developed to quickly monitor the transition from a primarily monomeric peptide into fibrils. Here we propose a novel method for both incubating and monitoring changes in Aβ aggregation by using modified NMR tubes, a microtube thermoshaker, and a fluorescence or UV-vis spectrometer. These NMR tubes are thin and cylindrical, which allows efficient heat transfer and orbital shaking. Our results demonstrate that our technique is both reliable and expedient when tracking Aβ fibrillization using fluorescence or turbidity assays, which presents an alternative for laboratories without specialized equipment for incubating peptide.

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Year:  2012        PMID: 23173070      PMCID: PMC3503345          DOI: 10.1021/cn300135n

Source DB:  PubMed          Journal:  ACS Chem Neurosci        ISSN: 1948-7193            Impact factor:   4.418


  34 in total

1.  Quantifying amyloid by congo red spectral shift assay.

Authors:  W E Klunk; R F Jacob; R P Mason
Journal:  Methods Enzymol       Date:  1999       Impact factor: 1.600

Review 2.  Twenty years of the Alzheimer's disease amyloid hypothesis: a genetic perspective.

Authors:  Rudolph E Tanzi; Lars Bertram
Journal:  Cell       Date:  2005-02-25       Impact factor: 41.582

3.  Multiple assembly pathways underlie amyloid-beta fibril polymorphisms.

Authors:  Claire Goldsbury; Peter Frey; Vesna Olivieri; Ueli Aebi; Shirley A Müller
Journal:  J Mol Biol       Date:  2005-09-16       Impact factor: 5.469

4.  Small molecule inhibitors of aggregation indicate that amyloid beta oligomerization and fibrillization pathways are independent and distinct.

Authors:  Mihaela Necula; Rakez Kayed; Saskia Milton; Charles G Glabe
Journal:  J Biol Chem       Date:  2007-02-06       Impact factor: 5.157

5.  Curcumin inhibits formation of amyloid beta oligomers and fibrils, binds plaques, and reduces amyloid in vivo.

Authors:  Fusheng Yang; Giselle P Lim; Aynun N Begum; Oliver J Ubeda; Mychica R Simmons; Surendra S Ambegaokar; Pingping P Chen; Rakez Kayed; Charles G Glabe; Sally A Frautschy; Gregory M Cole
Journal:  J Biol Chem       Date:  2004-12-07       Impact factor: 5.157

6.  A kinetic model for amyloid formation in the prion diseases: importance of seeding.

Authors:  J H Come; P E Fraser; P T Lansbury
Journal:  Proc Natl Acad Sci U S A       Date:  1993-07-01       Impact factor: 11.205

Review 7.  The aggregation and fibrillation of alpha-synuclein.

Authors:  Anthony L Fink
Journal:  Acc Chem Res       Date:  2006-09       Impact factor: 22.384

8.  Amyloid beta-protein fibrillogenesis. Detection of a protofibrillar intermediate.

Authors:  D M Walsh; A Lomakin; G B Benedek; M M Condron; D B Teplow
Journal:  J Biol Chem       Date:  1997-08-29       Impact factor: 5.157

9.  Alzheimer's Abeta peptides containing an isostructural backbone mutation afford distinct aggregate morphologies but analogous cytotoxicity. Evidence for a common low-abundance toxic structure(s)?

Authors:  Jan Bieschke; Sarah J Siegel; Yanwen Fu; Jeffery W Kelly
Journal:  Biochemistry       Date:  2007-12-14       Impact factor: 3.162

10.  Fibrillogenesis in Alzheimer's disease of amyloid beta peptides and apolipoprotein E.

Authors:  E M Castano; F Prelli; T Wisniewski; A Golabek; R A Kumar; C Soto; B Frangione
Journal:  Biochem J       Date:  1995-03-01       Impact factor: 3.857

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  1 in total

1.  Modification of Aβ Peptide Aggregation via Covalent Binding of a Series of Ru(III) Complexes.

Authors:  Luiza M F Gomes; Janaina C Bataglioli; Allison J Jussila; Jason R Smith; Charles J Walsby; Tim Storr
Journal:  Front Chem       Date:  2019-12-03       Impact factor: 5.221

  1 in total

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