4 research outputs found

    Synthetic β‑Barrel by Metal-Induced Folding and Assembly

    No full text
    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

    Synthetic β‑Barrel by Metal-Induced Folding and Assembly

    No full text
    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

    Mutual Induced Fit in a Synthetic Host–Guest System

    No full text
    Mutual induced fit is an important phenomenon in biological molecular recognition, but it is still rare in artificial systems. Here we report an artificial host–guest system in which a flexible calix[4]­arene is enclathrated in a dynamic self-assembled host and both molecules mutually adopt specific three-dimensional structures. NMR data revealed the conformational changes, and crystallographic studies clearly established the precise structures at each stage

    Synthetic β‑Barrel by Metal-Induced Folding and Assembly

    No full text
    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
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