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Synthetic β-barrel by metal-induced folding and assembly
Journal of the American Chemical Society ( IF 15.0 ) Pub Date : 2018-07-05 , DOI: 10.1021/jacs.8b04284
Motoya Yamagami 1 , Tomohisa Sawada 1 , Makoto Fujita 1
Affiliation  

The de novo construction of repeat proteins has received much attention from biologists and chemists, yet that of a β-barrel structure, one of the most well-known classes, has not been accomplished to date. Here, we report the first chemical construction of a β-barrel tertiary structure with a pore through a combination of peptide folding and metal-directed self-assembly. Coordination of zinc salts to an eight-residue peptide fragment bearing β-strand- and loop-forming sequences resulted in a β-barrel in which six-stranded cylindrical antiparallel β-sheets formed a hydrophobic pore with a specific shape.

中文翻译:

通过金属诱导折叠和组装合成 β-桶

重复蛋白的从头构建已受到生物学家和化学家的广泛关注,但迄今为止,β-桶结构(最著名的类别之一)的构建尚未完成。在这里,我们报告了通过肽折叠和金属定向自组装的组合首次化学构建具有孔的 β 桶三级结构。锌盐与带有 β 链和环形成序列的八残基肽片段的配位导致 β 桶,其中六链圆柱形反平行 β 折叠形成具有特定形状的疏水孔。
更新日期:2018-07-05
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