کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
5372322 | 1503980 | 2007 | 6 صفحه PDF | دانلود رایگان |

The formation of amyloid fibrils from insulin is investigated using drop-coating-deposition-Raman (DCDR) difference spectroscopy and atomic force microscopy (AFM). Fibrils formed using various co-solvents and heating cycles are found to induce the appearance of Raman difference peaks in the amide I (â¼Â 1675 cmâ 1), amide III (â¼Â 1220 cmâ 1), and peptide backbone (â¼Â 1010 cmâ 1), consistent with an increase in β-sheet content. Comparisons of results obtained from fibrils in either H2O or D2O suggest that the NH/ND stretch bands (at â¼Â 3300 cmâ 1/â¼Â 2400 cmâ 1) are also enhanced in intensity upon fibril formation. If there is any water trapped in the core of the fibrils its OH/OD Raman intensity is too small to be detected in the presence of the stronger NH/ND bands which appear in the same region. AFM is used to confirm the formation of fibrils of about 5 nm diameter (and various lengths).
Journal: Biophysical Chemistry - Volume 128, Issues 2â3, July 2007, Pages 150-155