Department of Applied Chemistry, School of Engineering , The University of Tokyo , 7-3-1 Hongo , Bunkyo-ku, Tokyo 113-8656 , Japan.
J Am Chem Soc. 2018 Jul 18;140(28):8644-8647. doi: 10.1021/jacs.8b04284. Epub 2018 Jul 9.
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.
从头构建重复蛋白质一直受到生物学家和化学家的关注，但到目前为止，还没有完成对其中最著名的一类β-桶结构的构建。在这里，我们报告了首次通过肽折叠和金属导向自组装的组合来构建具有孔的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形成β-桶，其中六股圆柱形反平行β-片形成具有特定形状的疏水性孔。
