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Reversibility of β-Amyloid Self-Assembly: Effects of pH and Added Salts Assessed by Fluorescence Photobleaching Recovery

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Department of Chemistry and Macromolecular Studies Group, Louisiana State University, Baton Rouge, Louisiana 70803
* To whom correspondence should be addressed. E-mail: [email protected]
Cite this: Biomacromolecules 2010, 11, 2, 341–347
Publication Date (Web):January 19, 2010
https://doi.org/10.1021/bm900833b
Copyright © 2010 American Chemical Society

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    Abstract

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    The 40-residue peptide isoform β-amyloid (Aβ1−40) is associated with Alzheimer’s disease. Although found in the tangles and fibrous mats that characterize the brain in advanced stages of the disease, the toxic form of Aβ is believed to be oligomers or “protofibrils”. Characterization of these fairly small structures in solution, especially in the presence of the much larger assemblies they also form, is a daunting task. Additionally, little is known about the rate of Aβ assembly or whether it can be triggered easily. Perhaps most importantly, the conditions for reversing assembly are not fully understood. Fluorescence photobleaching with modulation detection of the recovery profile is a sensitive and materials-efficient way to measure diffusers over a wide range of hydrodynamic sizes. The method does require attachment of a fluorescent label. Experiments to validate the use of 5-carboxyfluorescein-labeled Aβ(1−40) as a representative of the unlabeled, naturally occurring material included variation of photobleaching time and mixture of labeled and unlabeled materials. A dialysis cell facilitated rapid in situ changes in pH and salt conditions. Multiple steps and complex protocols can be explored with relative ease. Oligomeric aggregates were found by fluorescence photobleaching recovery to respond readily to pH and salt conditions. Changing these external cues leads to formation or disassembly of aggregates smaller than 100 nm within minutes.

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    Illustration of the graphical interface for the testing agreement between CONTIN and nonlinear, single-, or multiexponential fits. This material is available free of charge via the Internet at http://pubs.acs.org.

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    Cited By

    This article is cited by 11 publications.

    1. Jiali Du and Regina M. Murphy. Characterization of the Interaction of β-Amyloid with Transthyretin Monomers and Tetramers. Biochemistry 2010, 49 (38) , 8276-8289. https://doi.org/10.1021/bi101280t
    2. Jofre Seira Curto, Maria Rosario Fernandez, Josep Cladera, Núria Benseny-Cases, Natalia Sanchez de Groot. Aβ40 Aggregation under Changeable Conditions. International Journal of Molecular Sciences 2023, 24 (9) , 8408. https://doi.org/10.3390/ijms24098408
    3. Simon Alberti, Anthony A. Hyman. Biomolecular condensates at the nexus of cellular stress, protein aggregation disease and ageing. Nature Reviews Molecular Cell Biology 2021, 22 (3) , 196-213. https://doi.org/10.1038/s41580-020-00326-6
    4. Ferenc Bogár, Dóra Simon, Zsolt Bozsó, Tamás Janáky, Szilvia Veszelka, Andrea E. Tóth, Mária A. Deli, Attila Borics, Zoltán Násztor, Andrea Gyebrovszki, Botond Penke, Lívia Fülöp. Opposite effect of Ca2+/Mg2+ ions on the aggregation of native and precursor-derived Aβ42. Structural Chemistry 2015, 26 (5-6) , 1389-1403. https://doi.org/10.1007/s11224-015-0660-2
    5. . 5‐Carboxyfluorescein. 2015, 110-113. https://doi.org/10.1002/9781119007104.ch43
    6. Hellen Ishikawa‐Ankerhold, Richard Ankerhold, Gregor Drummen. Fluorescence Recovery After Photobleaching ( FRAP ). 2014https://doi.org/10.1002/9780470015902.a0003114
    7. Mariana Amaro, Thorben Wellbrock, David J. S. Birch, Olaf J. Rolinski. Inhibition of beta-amyloid aggregation by fluorescent dye labels. Applied Physics Letters 2014, 104 (6) https://doi.org/10.1063/1.4865197
    8. Hendrik Deschout, Koen Raemdonck, Jo Demeester, Stefaan C. De Smedt, Kevin Braeckmans. FRAP in Pharmaceutical Research: Practical Guidelines and Applications in Drug Delivery. Pharmaceutical Research 2014, 31 (2) , 255-270. https://doi.org/10.1007/s11095-013-1146-9
    9. Karen Pillay, Patrick Govender. A direct fluorescence‐based technique for cellular localization of amylin. Biotechnology and Applied Biochemistry 2013, 60 (4) , 384-392. https://doi.org/10.1002/bab.1113
    10. Wilda Helen, Piero de Leonardis, Rein V. Ulijn, Julie Gough, Nicola Tirelli. Mechanosensitive peptidegelation: mode of agitation controls mechanical properties and nano-scale morphology. Soft Matter 2011, 7 (5) , 1732-1740. https://doi.org/10.1039/C0SM00649A
    11. Gamal Rayan, Jean-Erik Guet, Nicolas Taulier, Frederic Pincet, Wladimir Urbach. Recent Applications of Fluorescence Recovery after Photobleaching (FRAP) to Membrane Bio-Macromolecules. Sensors 2010, 10 (6) , 5927-5948. https://doi.org/10.3390/s100605927

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