3 research outputs found
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 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
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
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