Format

Send to

Choose Destination
Nat Chem. 2016 Nov;8(11):1008-1014. doi: 10.1038/nchem.2556. Epub 2016 Jul 11.

Peptide tessellation yields micrometre-scale collagen triple helices.

Author information

1
Department of Biochemistry, University of Wisconsin-Madison, Madison, Wisconsin 53706, USA.
2
Department of Chemistry, University of Wisconsin-Madison, Madison, Wisconsin 53706, USA.

Abstract

Sticky-ended DNA duplexes can associate spontaneously into long double helices; however, such self-assembly is much less developed with proteins. Collagen is the most prevalent component of the extracellular matrix and a common clinical biomaterial. As for natural DNA, the ~103-residue triple helices (~300 nm) of natural collagen are recalcitrant to chemical synthesis. Here we show how the self-assembly of short collagen-mimetic peptides (CMPs) can enable the fabrication of synthetic collagen triple helices that are nearly a micrometre in length. Inspired by the mathematics of tessellations, we derive rules for the design of single CMPs that self-assemble into long triple helices with perfect symmetry. Sticky ends thus created are uniform across the assembly and drive its growth. Enacting this design yields individual triple helices that, in length, match or exceed those in natural collagen and are remarkably thermostable, despite the absence of higher-order association. The symmetric assembly of CMPs provides an enabling platform for the development of advanced materials for medicine and nanotechnology.

PMID:
27768103
PMCID:
PMC5123832
DOI:
10.1038/nchem.2556
[Indexed for MEDLINE]
Free PMC Article

Supplemental Content

Full text links

Icon for Nature Publishing Group Icon for PubMed Central
Loading ...
Support Center