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Molecular simulation of the primary and secondary structures of the Aβ(1-42)-peptide of Alzheimer's disease by Peter P. Mager is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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The major protein constituent of the deposits of Alzheimer's disease is the so-called amyloid ␤-peptide (A␤) which was derived from proteolysis of a large transmembrane amyloid precursor protein. Some physicochemical and biological properties of the A␤(1-42) peptide are described in this paper. Three functional areas of the soluble A␤(1-42) peptide were found: (i) a lipophilic region in the middle of the peptide (Lys16 to Ala21), (ii) a second lipophilic core at the end (Lys28 to Val40), and (iii) polarized and charged, solvent-exposed areas. Using molecule coordinates found experimentally by NMR-solution spectroscopy, subsequent Gasteiger-MM ϩ geometry optimization led to the result that the first lipophilic core has an ␣-helical structure which is stabilized by intramolecular hydrogen-bonding forces. The result is a loop-like molecule. The second lipophilic core has a ␤-sheet structure, and is able to form long-ranged, noncovalent, mainly hydrophobic forces with other ␤-sheets of A␤ peptides. The ␤-strands run in an antiparallel direction. The aggregates are highly stable and ordered. The negatively charged, solvent-exposed residues are potential sites for a crosslinking with mem

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Author

Peter P. Mager

Publisher

John Wiley and Sons; Wiley (John Wiley & Sons); John Wiley & Sons Inc.; Wiley (ISSN 0198-6325)

Published

1998

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)