Self-assembly of fiber-forming collagen mimetic peptides controlled by triple-helical nucleation

Biplab Sarkar, Lesley E.R. Oleary, Jeffrey D. Hartgerink

Research output: Contribution to journalArticlepeer-review

87 Scopus citations


Mimicking the multistep self-assembly of the fibrillar protein collagen is an important design challenge in biomimetic supramolecular chemistry. Utilizing the complementarity of oppositely charged domains in short collagen-like peptides, we have devised a strategy for the self-assembly of these peptides into fibers. The strategy depends on the formation of a staggered triple helical species facilitated by interchain charged pairs, and is inspired by similar sticky-ended fibrillation designs applied in DNA and coiled coil fibers. We compare two classes of collagen mimetic peptides with the same composition but different domain arrangements, and show that differences in their proposed nucleation events differentiates their fibrillation capabilities. Larger nucleation domains result in rapid fiber formation and eventual precipitation or gelation while short nucleation domains leave the peptide soluble for long periods of time. For one of the fiber-forming peptides, we elucidate the packing parameters by X-ray diffraction.

Original languageEnglish (US)
Pages (from-to)14417-14424
Number of pages8
JournalJournal of the American Chemical Society
Issue number41
StatePublished - Oct 15 2014
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Catalysis
  • General Chemistry
  • Biochemistry
  • Colloid and Surface Chemistry


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