Self-assembly of giant peptide nanobelts

Honggang Cui, Takahiro Muraoka, Andrew G. Cheetham, Samuel I. Stupp

Research output: Contribution to journalArticlepeer-review

359 Citations (Scopus)


Many alkylated peptide amphiphiles have been reported to self-assemble into cylindrical nanofibers with diameters on the order of a few nanometers and micrometer scale lengths; these nanostructures can be highly bioactive and are of great interest in many biomedical applications. We have discovered the sequences for these molecules that can eliminate all curvature from the nanostructures they form in water and generate completely flat nanobelts with giant dimensions relative to previously reported systems. The nanobelts have fairly monodisperse widths on the order of 150 nm and lengths of up to 0.1 mm. The sequences have an alternating sequence with hydrophobic and hydrophilic side chains and variations in monomer concentration generate a "broom" morphology with twisted ribbons that reveals the mechanism through which giant nanobelts form. Interestingly, a variation in pH generates reversibly periodic 2 nm grooves on the surfaces of the nanobelts. With proper functionalization, these nanostructures offer a novel architecture to present epitopes to cells for therapeutic applications.

Original languageEnglish
Pages (from-to)945-951
Number of pages7
JournalNano Letters
Issue number3
Publication statusPublished - 2009 Mar 11
Externally publishedYes

ASJC Scopus subject areas

  • Bioengineering
  • Chemistry(all)
  • Materials Science(all)
  • Condensed Matter Physics
  • Mechanical Engineering


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