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Structure of Aß(25–35) Peptide in Different Environments

Department of Chemistry, Vanderbilt University, Nashville, Tennessee 37235

Correspondence: Address reprint requests to Prasad L. Polavarapu, Tel.: 615-322-2836; Fax: 615-322-4936; E-mail: Prasad.L.Polavarapu{at}vanderbilt.edu.

The fragment Aß(25–35) of the Alzheimer's amyloid ß -peptide, like its full-length peptide Aß(1–42), has shown neurotoxic activities in cultured cells. The conformational preference of this important peptide is examined here in solution, gel, and film states (obtained with organic and aqueous solvents) by vibrational circular dichroism spectroscopy for the first time. For comparative studies, vibrational absorption and electronic circular dichroism measurements were also carried out under identical conditions. The peptide was found to adopt ß-sheet and ß-turn structures, with their relative proportions changing in different environments.

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