Supramolecular control of self-assembling terthiophene-peptide conjugates through the amino acid side chain
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.
- Authors:
-
- NWU
- Publication Date:
- Research Org.:
- Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
- Sponsoring Org.:
- National Science Foundation (NSF)
- OSTI Identifier:
- 1059533
- Resource Type:
- Journal Article
- Journal Name:
- ChemComm
- Additional Journal Information:
- Journal Volume: 48; Journal Issue: 78; Journal ID: ISSN 1359-7345
- Publisher:
- Royal Society of Chemistry
- Country of Publication:
- United States
- Language:
- ENGLISH
Citation Formats
Lehrman, Jessica A., Cui, Honggang, Tsai, Wei-Wen, Moyer, Tyson J., and Stupp, Samuel I. Supramolecular control of self-assembling terthiophene-peptide conjugates through the amino acid side chain. United States: N. p., 2013.
Web. doi:10.1039/C2CC34375D.
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. United States. https://doi.org/10.1039/C2CC34375D
Lehrman, Jessica A., Cui, Honggang, Tsai, Wei-Wen, Moyer, Tyson J., and Stupp, Samuel I. 2013.
"Supramolecular control of self-assembling terthiophene-peptide conjugates through the amino acid side chain". United States. https://doi.org/10.1039/C2CC34375D.
@article{osti_1059533,
title = {Supramolecular control of self-assembling terthiophene-peptide conjugates through the amino acid side chain},
author = {Lehrman, Jessica A. and Cui, Honggang and Tsai, Wei-Wen and Moyer, Tyson J. and Stupp, Samuel I.},
abstractNote = {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.},
doi = {10.1039/C2CC34375D},
url = {https://www.osti.gov/biblio/1059533},
journal = {ChemComm},
issn = {1359-7345},
number = 78,
volume = 48,
place = {United States},
year = {Tue Jul 30 00:00:00 EDT 2013},
month = {Tue Jul 30 00:00:00 EDT 2013}
}
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