Synthetic β‑Barrel by Metal-Induced Folding and Assembly

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...

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Veröffentlicht in:Journal of the American Chemical Society 2018-07, Vol.140 (28), p.8644-8647
Hauptverfasser: Yamagami, Motoya, Sawada, Tomohisa, Fujita, Makoto
Format: Artikel
Sprache:eng
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Zusammenfassung: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.
ISSN:0002-7863
1520-5126
DOI:10.1021/jacs.8b04284