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Formation Kinetics and Structural Features of Beta‐Amyloid Aggregates by Sedimented Solute NMR
Author(s) -
Bertini Ivano,
Gallo Gianluca,
Korsak Magdalena,
Luchinat Claudio,
Mao Jiafei,
Ravera Enrico
Publication year - 2013
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201300141
Subject(s) - kinetics , in situ , ultracentrifuge , chemistry , monomer , biomolecule , magic angle spinning , amyloid (mycology) , analytical ultracentrifugation , peptide , biophysics , nuclear magnetic resonance spectroscopy , biochemistry , stereochemistry , organic chemistry , polymer , biology , inorganic chemistry , physics , quantum mechanics
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.