Protein Assembly

Artificial β-barrel pores

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Science  03 Aug 2018:
Vol. 361, Issue 6401, pp. 464-465
DOI: 10.1126/science.361.6401.464-g

The de novo construction of proteins from peptide fragments that assemble into β-barrel structures, as opposed to α-helix or α/β folds, is challenging. Yamagami et al. show that six octapeptides, terminated with pyridyl groups, assemble into an antiparallel β-barrel structure when coordinated with ZnI2 linkers. The peptides contain a phenylalanine-valine-phenylalanine-valine sequence with a high propensity for forming β-sheets linked to a proline-glycine-proline sequence that forms a loop. The crystal structure reveals the formation of a pore lined with the hydrophobic isopropyl side chains of the valine residues.

J. Am. Chem. Soc. 10.1021/jacs.8b04284 (2018).

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