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Eur. J. Mass Spectrom. DOI: 10.1255/ejms.598

Contact regions in the dimer of Alzheimer β-amyloid domain [1-28] studied by mass spectrometry

Aiqun Li and Catherine Fenselau
Department of Chemistry and Biochemistry, University of Maryland Baltimore County, Catonsville, MD 21250, USA

ABSTRACT:
Information is provided about the amino acid residues in the [1-28] domain of the Alzheimer β-amyloid protein, which participate in interstrand pairing and initiate fibillogenesis. The study was carried out using electrospray ionization on a four sector mass spectrometer, measuring kinetic energy release for a fragmentation process, and modeling the transition state with molecular dynamics calculations. . The results eliminate the sequence [11-24] proposed earlier as the central core, and are consistent with, but do not distinguish between, residues [17-28] and [17-23] proposed by others based on biochemical studies.

Keywords: amyloid dimerization, Interstrand, pairing, four sector mass spectrometry

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