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Biochem Biophys Res Commun. 1995 Jan 17;206(2):718-23.

Stabilization of secondary structure of Alzheimer beta-protein by aluminum(III) ions and D-Asp substitutions.

Author information

1
Department of Chemistry and Biochemistry, University of Alaska Fairbanks, Fairbanks 99775.

Abstract

The CD spectra of the D-Asp substituted analogs of amyloid peptides, beta 6-25 and beta 1-40, showed a distinct blue-shift on Al3+ complexation. The influence of Al3+ coordination was most significant on the triply substituted beta 1-40 (D-Asp 1,7,23). This analog showed a reduction of the minima near 210nm and a simultaneous increase in the maxima near 200nm as compared to the native L-Asp beta 1-40. These observations suggest that Al3+ interaction with D-Asp induces the peptide backbone to increase its antiparallel beta-sheet character. D-Asp substitution and chelation by Al3+ lead to increased stability of higher molecular weight species of beta 1-40, and thereby could increase the toxicity of the Alzheimer amyloid protein.

PMID:
7826392
DOI:
10.1006/bbrc.1995.1101
[Indexed for MEDLINE]

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