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Fourier transform infrared spectroscopy used to evidence the prevention of beta-sheet formation of amyloid beta(1-40) peptide by a short amyloid fragment.

Reflectance Fourier transform infrared (FT-IR) microspectroscopy was applied to study the prevention of beta-sheet formation of amyloid beta (Abeta)(1-40) peptide by co-incubation with a hexapeptide containing a KLVFF sequence (Abeta(15-20) fragment). Second-derivative spectral analysis was used to locate the position of the overlapping components of the amide I band of Abeta peptide and assigned them to different secondary components. The result indicates that each intact sample of Abeta(15-20) fragment or Abeta(1-40) peptide previously incubated in distilled water at 37 degrees C transformed their secondary structure from 1649 (1651) or 1653cm(-1) to 1624cm(-1), suggesting the transformation from alpha-helix and/or random coil structures to beta-sheet structure. By co-incubating both samples with different molar ratio in distilled water at 37 degrees C, the structural transformation was not found for Abeta(1-40) peptide after 24h-incubation. But the beta-sheet formation of Abeta(1-40) peptide after 48h-incubation was evidenced from the appearance of the IR peak at 1626cm(-1) by adding a little amount of Abeta(15-20) fragment. There was no beta-sheet formation of Abeta(1-40) peptide after addition with much amount of Abeta(15-20) fragment, however, suggesting the higher amount of Abeta(15-20) fragment used might inhibit the beta-sheet formation of Abeta(1-40) peptide. The more Abeta(15-20) fragment used made the more stable structure of Abeta(1-40) peptide and the less beta-sheet formation of Abeta(1-40) peptide. The study indicates that the reflectance FT-IR microspectroscopy can easily evidence the prevention of beta-sheet formation of Abeta(1-40) peptide by a short amyloid fragment.