Solubilization of beta-amyloid-(1-42)-peptide: reversing the beta-sheet conformation induced by aluminum with silicates.

DOI Web Site 被引用文献2件
  • G D Fasman
    Graduate Department of Biochemistry, Brandeis University, Waltham, MA 02254.
  • A Perczel
    Graduate Department of Biochemistry, Brandeis University, Waltham, MA 02254.
  • C D Moore
    Graduate Department of Biochemistry, Brandeis University, Waltham, MA 02254.

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<jats:p>Plaques are one of the two lesions found in the brain of patients with Alzheimer disease. Using a synthetic peptide corresponding to rat beta-amyloid-(1-42) (beta A4), circular dichroism (CD) analyses were performed to examine the effect of Na4SiO4 on the conformational state produced by Al3+. A previous study on fragments of neuronal proteins involved in tangle formation had shown a conformational transition from a beta-pleated sheet to a soluble random coil upon addition of Na4SiO4. In the present study, CD measurements showed that the beta-pleated sheet conformation of beta A4 induced by Al3+ was reversed to the random coil soluble form by the addition of Na4SiO4. The tight binding of SiO4(4-) with Al3+ provides the mechanism for this transition. These results provide insight into the role of aluminum in the Alzheimer diseased brain and suggests that investigation of the use of silicates as a therapeutic agent.</jats:p>

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