The structure and dynamics of the Alzheimer's disease beta-amyloid (1-40) peptide and its adducts with
aluminum in aqueous solution are investigated using classical molecular dynamics simulations. The calculations indicate (i) that the peptide is stable in water solution and (ii) that Al**3+ does not destabilize the secondary
structure of the peptide. The formation of peptide-peptide cross links may be the cause of the Al-promoted
peptide aggregation found experimentally.
By: P. Carloni
Published in: RZ2957 in 1997
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