Programmable Assembly of Peptide Amphiphile via Noncovalent-to-Covalent Bond Conversion

Kohei Sato, Wei Ji, Liam C. Palmer, Benjamin Weber, Matthias Barz, Samuel I Stupp

Research output: Contribution to journalArticle

29 Citations (Scopus)

Abstract

Controlling the number of monomers in a supramolecular polymer has been a great challenge in programmable self-assembly of organic molecules. One approach has been to make use of frustrated growth of the supramolecular assembly by tuning the balance of attractive and repulsive intermolecular forces. We report here on the use of covalent bond formation among monomers, compensating for intermolecular electrostatic repulsion, as a mechanism to control the length of a supramolecular nanofiber formed by self-assembly of peptide amphiphiles. Circular dichroism spectroscopy in combination with dynamic light scattering, size-exclusion chromatography, and transmittance electron microscope analyses revealed that hydrogen bonds between peptides were reinforced by covalent bond formation, enabling the fiber elongation. To examine these materials for their potential biomedical applications, cytotoxicity of nanofibers against C2C12 premyoblast cells was tested. We demonstrated that cell viability increased with an increase in fiber length, presumably because of the suppressed disruption of cell membranes by the fiber end-caps.

Original languageEnglish
Pages (from-to)8995-9000
Number of pages6
JournalJournal of the American Chemical Society
Volume139
Issue number26
DOIs
Publication statusPublished - Jul 5 2017

ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)
  • Biochemistry
  • Colloid and Surface Chemistry

Fingerprint Dive into the research topics of 'Programmable Assembly of Peptide Amphiphile via Noncovalent-to-Covalent Bond Conversion'. Together they form a unique fingerprint.

  • Cite this