Formation Kinetics and Structural Features of Beta-Amyloid Aggregates by Sedimented Solute NMR

被引：36

作者：

Bertini, Ivano ^{[1
,2
,3
]}

Gallo, Gianluca ^{[1
,4
]}

Korsak, Magdalena ^{[1
,2
]}

Luchinat, Claudio ^{[1
,3
,4
]}

Mao, Jiafei ^{[1
,3
]}

Ravera, Enrico ^{[1
,4
]}

机构：

[1] Univ Florence, Magnet Resonance Ctr CERM, I-50019 Sesto Fiorentino, Italy

[2] Giotto Biotech, I-50019 Sesto Fiorentino, Italy

[3] Fdn Farmacogenom FiorGen Onlus, I-50019 Sesto Fiorentino, Italy

[4] Univ Florence, Dept Chem Ugo Schiff, I-50019 Sesto Fiorentino, Italy

来源：

CHEMBIOCHEM | 2013年 / 14卷 / 14期

关键词：

centrifugation; kinetics; oligomerization; sedimentation; solid-state NMR spectroscopy; SOLID-STATE NMR; ALZHEIMERS-DISEASE; PROTEIN OLIGOMERIZATION; POLARIZATION TRANSFER; HYDROGEN-EXCHANGE; MASS-SPECTROMETRY; FIBRILS; SPECTROSCOPY; ULTRACENTRIFUGATION; INTERMEDIATE;

D O I：

10.1002/cbic.201300141

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The accumulation of soluble toxic beta-amyloid (A beta) 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 A beta 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 A beta assemblies.

引用

页码：1891 / 1897

页数：7

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