Vesicle-Bound Alpha-Synuclein: Are the Helices Anti-Parallel or Extended?

Drescher, Malte; Rooijen, Bart D. van; Veldhuis, Gertjan; Godschalk, Frans; Milikisyants, Sergey; Subramaniam, Vinod; Huber, Martina

doi:10.1016/j.bpj.2009.12.1405

Biophysical Journal

2010

DOI: 10.1016/j.bpj.2009.12.1405

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Vesicle-Bound Alpha-Synuclein: Are the Helices Anti-Parallel or Extended?

Malte Drescher

Bart D. van Rooijen

Gertjan Veldhuis

et al.

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“…EPR spectroscopy is a technique for studying chemical species with unpaired electrons that has recently shown to be an efficient bioanalytical tool for determination of molecular distances and molecular size estimations from spin motion measurements [24][25][26][27][28][29][30]. This technique has recently shown high sensitivity compared to the traditional techniques for protein structure determination, such as NMR spectroscopy [31].…”

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Structural characterization of ß-amyloid oligomer-aggregates by ion mobility mass spectrometry and electron spin resonance spectroscopy

et al. 2009

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Formation and accumulation of fibrillar plaques and aggregates of beta-amyloid peptide (Abeta) in brain have been recognized as characteristics of Alzheimer's disease (AD). Oligomeric aggregates of Ass are considered critical intermediates leading to progressive neurodegeneration; however, molecular details of the oligomerization and aggregation pathway and the structures of Abeta-oligomers are hitherto unclear. Using an in vitro fibril formation procedure of Abeta(1-40), beta-amyloid aggregates were prepared and insoluble aggregates separated from soluble products by centrifugation. In this study, ion mobility mass spectrometry (IM-MS) was applied in combination with electron paramagnetic resonance spectroscopy (EPR) to the identification of the components of Abeta-oligomers, and to their structural and topographical characterization. The formation of Abeta-oligomers and aggregates was monitored by gel electrophoresis, and Abeta-oligomer bands were identified by in-gel tryptic digestion and matrix-assisted laser desorption ionization-mass spectrometry (MALDI-MS) to consist predominantly of Abeta(1-40) peptide. First, ion mobility-MS studies of soluble Abeta-aggregates prepared by incubation for 5 days were performed on a quadrupole time-of-flight mass spectrometer and revealed (1) the presence of at least two different conformational states, and (2), the formation of Met-35 oxidized products. For estimation of the size of Abeta-aggregates using EPR spectroscopy, a modified Abeta(1-40) peptide containing an additional N-terminal cysteine residue was prepared, and a 3-(2-iodoacetamido)-2,2,5,5-tetramethyl-1-pyrrolidinyloxy radical spin label derivative (IPSL) was coupled by S-alkylation. The EPR spectra of the spin-labeled Cys-Abeta(1-40) oligomers were matched with spectra simulations using a multi-component simulation strategy, resulting in complete agreement with the gel electrophoresis results.

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Structural characterization of ß-amyloid oligomer-aggregates by ion mobility mass spectrometry and electron spin resonance spectroscopy

et al. 2009

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Vesicle-Bound Alpha-Synuclein: Are the Helices Anti-Parallel or Extended?

Cited by 1 publication

References 0 publications

Structural characterization of ß-amyloid oligomer-aggregates by ion mobility mass spectrometry and electron spin resonance spectroscopy

Structural characterization of ß-amyloid oligomer-aggregates by ion mobility mass spectrometry and electron spin resonance spectroscopy

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