X-ray Crystallographic Structure of a Giant Double-Walled Peptide Nanotube Formed by a Macrocyclic β-Sheet Containing Aβ16–22
| Autor: | Stephanie P. Le, James S. Nowick, Kelsey A. Corro, Kevin H. Chen |
|---|---|
| Rok vydání: | 2017 |
| Předmět: |
chemistry.chemical_classification
Nanotube Nanostructure 010405 organic chemistry Chemistry Beta sheet Peptide General Chemistry Crystal structure 010402 general chemistry 01 natural sciences Biochemistry Catalysis 0104 chemical sciences Supramolecular assembly Crystallography Colloid and Surface Chemistry Honeycomb Hexagonal lattice |
| Zdroj: | Journal of the American Chemical Society. 139:8102-8105 |
| ISSN: | 1520-5126 0002-7863 |
| DOI: | 10.1021/jacs.7b03890 |
| Popis: | This paper describes the supramolecular assembly of a macrocyclic β-sheet containing residues 16–22 of the β-amyloid peptide, Aβ. X-ray crystallography reveals that the macrocyclic β-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 β-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. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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