Supramolecular control of self-assembling terthiophene-peptide conjugates through the amino acid side chain

Jessica A. Lehrman, Honggang Cui, Wei Wen Tsai, Tyson J. Moyer, Samuel I Stupp

Research output: Contribution to journalArticle

33 Citations (Scopus)

Abstract

The self-assembly of oligothiophene-peptide conjugates can be directed through the systematic variation of the peptide sequence into different nanostructures, including flat spicules, nanotubes, spiral sheets, and giant, flat sheets. Furthermore, the assembly of these molecules is not controlled by steric interactions between the amino acid side chains.

Original languageEnglish
Pages (from-to)9711-9713
Number of pages3
JournalChemical Communications
Volume48
Issue number78
DOIs
Publication statusPublished - Oct 9 2012

Fingerprint

Peptides
Amino acids
Amino Acids
Self assembly
Nanotubes
Nanostructures
Molecules
alpha-terthienyl

ASJC Scopus subject areas

  • Metals and Alloys
  • Materials Chemistry
  • Surfaces, Coatings and Films
  • Electronic, Optical and Magnetic Materials
  • Ceramics and Composites
  • Catalysis
  • Chemistry(all)

Cite this

Supramolecular control of self-assembling terthiophene-peptide conjugates through the amino acid side chain. / Lehrman, Jessica A.; Cui, Honggang; Tsai, Wei Wen; Moyer, Tyson J.; Stupp, Samuel I.

In: Chemical Communications, Vol. 48, No. 78, 09.10.2012, p. 9711-9713.

Research output: Contribution to journalArticle

Lehrman, Jessica A. ; Cui, Honggang ; Tsai, Wei Wen ; Moyer, Tyson J. ; Stupp, Samuel I. / Supramolecular control of self-assembling terthiophene-peptide conjugates through the amino acid side chain. In: Chemical Communications. 2012 ; Vol. 48, No. 78. pp. 9711-9713.
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