The de novo construction of repeat proteins has received much attention from biologists and chemists, yet that of a beta-barrel structure, one of the most well-known classes, has not been accomplished to date. Here, we report the first chemical construction of a beta-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 beta-strand- and loop-forming sequences resulted in a beta-barrel in which six-stranded cylindrical antiparallel beta-sheets formed a hydrophobic pore with a specific shape.