Contact regions in the dimer of Alzheimer β-amyloid domain [1

Eur. J. Mass Spectrom. 10, 309–316 (2004)
DOI: 10.1255/ejms.642

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. E-mail: fenselau@umail.umd.edu

ABSTRACT:

Information is provided about the amino acid residues in the [1–28] domain of the Alzheimer b-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, kinetic energy release

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