Lakeland College, Natural Sciences Division, Sheboygan, WI 53082
Amyloid aggregation of a nine residue peptide, known as Fpeptide, whose sequence (KLVFFAEDV) was derived from the Amyloid Beta protein has been prevented when the Fpeptide is incubated with inositol in aqueous solution. Attenuated Total Reflectance (ATR) FTIR spectra indicates a conformational change in the secondary structure of the Fpeptide when the Fpeptide is incubated with inositol at specific inositol concentrations. In addition, when Fpeptide is incubated with inositol Congo Red Microscopy shows no green birefringence which suggests that no amyloid fibrils are present in the peptide aggregate. Isotopic enhanced ATR-FTIR spectroscopy has been used to probe the changes in the conformation of Fpeptide in the presence of inositol. The results of this study suggest that inositol could be used to prevent amyloid aggregation in pharmaceutical applications and perhaps in biological systems as well
[Abstract (DOC)]