Analysis of insulin amyloid fibrils by Raman spectroscopy
Analysis of insulin amyloid fibrils by Raman spectroscopy
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DOI：
10.1016/j.bpc.2007.03.012
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发表时间：
2007-07-01
影响因子：
3.8
通讯作者：
Ben-Amotz, Dor
中科院分区：
文献类型：
--
作者：
Ortiz, Corasi;Zhang, Dongmao;Ben-Amotz, Dor
用滴涂沉积拉曼（DCDR）差谱和原子力显微镜（AFM）研究了胰岛素淀粉样纤维的形成。发现使用各种共溶剂和加热循环形成的原纤维诱导酰胺1（类似于1675 cm（-1））、酰胺III（类似于1220 cm（-1））和肽主链（类似于1010 cm（-1））中出现拉曼差异峰，这与β-折叠含量的增加一致。从H2O或D2 O中的原纤维获得的结果的比较表明，NH/ND拉伸带（在类似于3300 cm（-1）/类似于2400 cm（-1）处）在原纤维形成时强度也增强。如果有任何水被截留在原纤维的核心中，则其OH/OD拉曼强度太小而不能在出现在相同区域中的较强NH/ND带的存在下被检测到。AFM用于确认约5 nm直径（和各种长度）的原纤维的形成。(c)2007 Elsevier B. V.保留所有权利。
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 1 (similar to 1675 cm(-1)), amide III (similar to 1220 cm(-1)), and peptide backbone (similar to 1010 cm(-1)), consistent with an increase in beta-sheet content. Comparisons of results obtained from fibrils in either H2O or D2O suggest that the NH/ND stretch bands (at similar to 3300 cm(-1)/similar to 2400 cm(-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). (c) 2007 Elsevier B.V. All rights reserved.