Contact regions in the dimer of Alzheimer beta-amyloid domain [1-28] studied by mass spectrometry.
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.
Li
Aiqun
A
Department of Chemistry and Biochemistry, University of Maryland Baltimore County, Catonsville, MD 21250, USA.
Fenselau
Catherine
C
D000544:Alzheimer Disease / Q000378:metabolism*; D000595:Amino Acid Sequence; D016229:Amyloid beta-Peptides / Q000737:chemistry* / Q000378:metabolism*; D001665:Binding Sites; D019281:Dimerization; D007700:Kinetics; D008969:Molecular Sequence Data; D020836:Protein Structure, Quaternary; D017434:Protein Structure, Tertiary; D021241:Spectrometry, Mass, Electrospray Ionization
D016229:Amyloid beta-Peptides