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Collagen mimics snap into place

Peptides form self-assembled fibers that are long enough to be clinically useful

by Celia Henry Arnaud
July 18, 2016 | A version of this story appeared in Volume 94, Issue 29

Collagen, the predominant structural protein in animals, is a common biomaterial for clinical applications. Natural collagen is a triple-helix protein made of repeating proline-rich tripeptides. Posttranslational modifications make human collagen difficult to produce. And nonhuman collagens can trigger allergic reactions, complicating clinical use. So researchers have tried to make synthetic collagen-mimetic peptides instead. So far, these have been restricted to short pieces that aren’t particularly useful. Now, Ronald T. Raines and coworkers at the University of Wisconsin, Madison, have designed collagen-mimetic peptides that can self-assemble into symmetric triple-helix fibers that are almost 1 μm long, which is on the length scale of human collagen fibers (Nat. Chem. 2016, DOI: 10.1038/nchem.2556). Raines and coworkers achieve such long fibers by using peptides that have regularly spaced lysine and aspartic acid residues along with the proline, 4-hydroxyproline, and glycine that are found in natural collagen. The lysine and aspartic acid residues form salt bridges between neighboring strands and hold the peptides in place like tiles. They find that peptides must have 3n ± 1 tripeptide repeat units to assemble symmetrically.

Scheme showing assembly of collagen-mimetic peptides.
Credit: Adapted from Nat. Chem.
Collagen-mimetic peptides with lysine- and aspartic acid-containing regions (blue and red, respectively) self-assemble to form homotrimers with “sticky ends.” The homotrimers are held together by salt bridges between lysine and aspartic acid residues on adjacent peptides. The trimers then self-assemble to form fibers about 1 μm long.


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