Abstract
We study the self-assembly of peptide amphiphile (PA) molecules, which is governed by hydrophobic interactions between alkyl tails and a network of hydrogen bonds between peptide blocks. We demonstrate that the interplay between these two interactions results in the formation of assemblies of different morphology, in particular, single β-sheets connected laterally by hydrogen bonds, stacks of parallel β-sheets, spherical micelles, micelles with β-sheets in the corona, and long cylindrical fibers. We characterize the size distribution of the aggregates as a function of the molecular interactions. Our results suggest that the formation of nanofibers of peptide amphiphiles obeys an open association model, which resembles living polymerization.
| Original language | English |
|---|---|
| Pages (from-to) | 2326-2334 |
| Number of pages | 9 |
| Journal | Journal of Physical Chemistry B |
| Volume | 112 |
| Issue number | 8 |
| DOIs | |
| Publication status | Published - Feb 28 2008 |
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ASJC Scopus subject areas
- Physical and Theoretical Chemistry
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Molecular simulation study of peptide amphiphile self-assembly. / Velichko, Yuri S.; Stupp, Samuel I; De La Cruz, Monica Olvera.
In: Journal of Physical Chemistry B, Vol. 112, No. 8, 28.02.2008, p. 2326-2334.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Molecular simulation study of peptide amphiphile self-assembly
AU - Velichko, Yuri S.
AU - Stupp, Samuel I
AU - De La Cruz, Monica Olvera
PY - 2008/2/28
Y1 - 2008/2/28
N2 - We study the self-assembly of peptide amphiphile (PA) molecules, which is governed by hydrophobic interactions between alkyl tails and a network of hydrogen bonds between peptide blocks. We demonstrate that the interplay between these two interactions results in the formation of assemblies of different morphology, in particular, single β-sheets connected laterally by hydrogen bonds, stacks of parallel β-sheets, spherical micelles, micelles with β-sheets in the corona, and long cylindrical fibers. We characterize the size distribution of the aggregates as a function of the molecular interactions. Our results suggest that the formation of nanofibers of peptide amphiphiles obeys an open association model, which resembles living polymerization.
AB - We study the self-assembly of peptide amphiphile (PA) molecules, which is governed by hydrophobic interactions between alkyl tails and a network of hydrogen bonds between peptide blocks. We demonstrate that the interplay between these two interactions results in the formation of assemblies of different morphology, in particular, single β-sheets connected laterally by hydrogen bonds, stacks of parallel β-sheets, spherical micelles, micelles with β-sheets in the corona, and long cylindrical fibers. We characterize the size distribution of the aggregates as a function of the molecular interactions. Our results suggest that the formation of nanofibers of peptide amphiphiles obeys an open association model, which resembles living polymerization.
UR - http://www.scopus.com/inward/record.url?scp=40549086613&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=40549086613&partnerID=8YFLogxK
U2 - 10.1021/jp074420n
DO - 10.1021/jp074420n
M3 - Article
VL - 112
SP - 2326
EP - 2334
JO - Journal of Physical Chemistry B
JF - Journal of Physical Chemistry B
SN - 1520-6106
IS - 8
ER -