5vf1

Publication Abstract from PubMed

This paper describes the supramolecular assembly of a macrocyclic beta-sheet containing residues 16-22 of the beta-amyloid peptide, Abeta. X-ray crystallography reveals that the macrocyclic beta-sheet assembles to form double-walled nanotubes, with an inner diameter of 7 nm and outer diameter of 11 nm. The inner wall is composed of an extended network of hydrogen-bonded dimers. The outer wall is composed of a separate extended network of beta-barrel-like tetramers. These large peptide nanotubes pack into a hexagonal lattice that resembles a honeycomb. The complexity and size of the peptide nanotubes rivals some of the largest tubular biomolecular assemblies, such as GroEL and microtubules. These observations demonstrate that small amyloidogenic sequences can be used to build large nanostructures.

X-ray Crystallographic Structure of a Giant Double-Walled Peptide Nanotube Formed by a Macrocyclic beta-Sheet Containing Abeta16-22.,Chen KH, Corro KA, Le SP, Nowick JS J Am Chem Soc. 2017 Jun 21;139(24):8102-8105. doi: 10.1021/jacs.7b03890. Epub, 2017 Jun 13. PMID:28598147^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.