Formation Kinetics and Structural Features of Beta‐Amyloid Aggregates by Sedimented Solute NMR |
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| Authors: | Gianluca Gallo Magdalena Korsak Prof. Claudio Luchinat Dr. Jiafei Mao Dr. Enrico Ravera |
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| Affiliation: | 1. Magnetic Resonance Center (CERM), University of Florence, Via L. Sacconi 6, 50019 Sesto Fiorentino (Italy);2. Department of Chemistry “Ugo Schiff”, University of Florence, Via della Lastruccia 3, 50019 Sesto Fiorentino (Italy);3. Giotto Biotech, Via Madonna del Piano 6, 50019 Sesto Fiorentino (Italy);4. Fondazione Farmacogenomica FiorGen onlus Via L. Sacconi 6, 50019 Sesto Fiorentino (Italy);5. Current address: Goethe Universit?t, Max‐von‐Laue‐Strasse 9, Biozentrum N202, 60438 Frankfurt am Main (Germany) |
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| Abstract: | The accumulation of soluble toxic beta‐amyloid (Aβ) aggregates is an attractive hypothesis for the role of this peptide in the pathology of Alzheimer's disease. We have introduced sedimentation through ultracentrifugation, either by magic angle spinning (in situ) or preparative ultracentrifuge (ex situ), to immobilize biomolecules and make them amenable for solid‐state NMR studies (SedNMR). In situ SedNMR is used here to address the kinetics of formation of soluble Aβ assemblies by monitoring the disappearance of the monomer and the appearance of the oligomers simultaneously. Ex situ SedNMR allows us to select different oligomeric species and to reveal atomic‐level structural features of soluble Aβ assemblies. |
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| Keywords: | centrifugation kinetics oligomerization sedimentation solid‐state NMR spectroscopy |
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