Coassembly of amphiphiles with opposite peptide polarities into nanofibers

Heather A. Behanna, Jack J.J.M. Donners, Alex C. Gordon, Samuel I. Stupp*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

288 Scopus citations


The design, synthesis, and characterization of "reverse" peptide amphiphiles (PAs) with free N-termini is described. Use of an unnatural amino acid modified with a fatty acid tail allows for the synthesis of this new class of PA molecules. The mixing of these molecules with complementary ones containing a free C-terminus results in coassembled structures, as demonstrated by circular dichroism and NOE/NMR spectroscopy. These assemblies show unusual thermal stability when compared to assemblies composed of only one type of PA molecule. This class of reverse PAs has made it possible to create biologically significant assemblies with free N-terminal peptide sequences, which were previously inaccessible, including those derived from phage display methodologies.

Original languageEnglish (US)
Pages (from-to)1193-1200
Number of pages8
JournalJournal of the American Chemical Society
Issue number4
StatePublished - Feb 2 2005

ASJC Scopus subject areas

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


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