Structural model of the amyloid fibril formed by β2-microglobulin #21-31 fragment based on vibrational spectroscopy
Structural model of the amyloid fibril formed by β2-microglobulin #21-31 fragment based on vibrational spectroscopy
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DOI：
10.1021/ja050844o
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发表时间：
2005-06-08
影响因子：
15
通讯作者：
Kitagawa, T
中科院分区：
文献类型：
--
作者：
Hiramatsu, H;Goto, Y;Kitagawa, T
由β2-微球蛋白的#21−31片段形成的淀粉样原纤维的结构模型是根据对特异性13 C标记的肽原纤维的显微镜IR测量和分散的原纤维溶液的拉曼光谱提出的。 13 C位移的酰胺频率表明了标记残基的二级结构。红外光谱表明F22和V27之间的区域形成具有延伸的β-折叠结构的核心部分。拉曼光谱表明在 C25 残基之间形成了具有二硫键的二聚体。
A structural model of amyloid fibril formed by the #21−31 fragment of β2-microglobulin is proposed from microscope IR measurements on specifically13C-labeled peptide fibrils and Raman spectra of the dispersed fibril solution. The13C-shifted amide frequency indicated the secondary structure of the labeled residues. The IR spectra have demonstrated that the region between F22 and V27 forms the core part with the extended β-sheet structure. Raman spectra indicated the formation of a dimer with a disulfide bridge between C25 residues.