Abstract
Peptide amphiphile molecules (PAs) developed in our laboratory self-assemble from aqueous media into three-dimensional networks of bioactive nanofibers. Multiple non-covalent interactions promote assembly of the supramolecular nanofibers and ultimately determine the bulk physical properties of the macroscopic gels. In this study, we use oscillatory rheology, Fourier-transform infrared spectroscopy, and circular-dichroism spectroscopy to better understand the assembly mechanism of a typical PA molecule known as PA-1. Self-assembly of PA-1 is triggered by counterion screening and stabilized by van der Waals and hydrophobic forces, ionic bridging, and coordination and hydrogen bonding. The concentration, electronic structure, and hydration of counterions significantly influence self-assembly and gel mechanical properties.
| Original language | English |
|---|---|
| Pages (from-to) | 499-508 |
| Number of pages | 10 |
| Journal | Advanced Functional Materials |
| Volume | 16 |
| Issue number | 4 |
| DOIs | |
| Publication status | Published - Mar 3 2006 |
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ASJC Scopus subject areas
- Electronic, Optical and Magnetic Materials
- Materials Science(all)
- Condensed Matter Physics
- Physics and Astronomy (miscellaneous)
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Intermolecular forces in the self-assembly of peptide amphiphile nanofibers. / Stendahl, John C.; Rao, Mukti S.; Guler, Mustafa O.; Stupp, Samuel I.
In: Advanced Functional Materials, Vol. 16, No. 4, 03.03.2006, p. 499-508.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Intermolecular forces in the self-assembly of peptide amphiphile nanofibers
AU - Stendahl, John C.
AU - Rao, Mukti S.
AU - Guler, Mustafa O.
AU - Stupp, Samuel I
PY - 2006/3/3
Y1 - 2006/3/3
N2 - Peptide amphiphile molecules (PAs) developed in our laboratory self-assemble from aqueous media into three-dimensional networks of bioactive nanofibers. Multiple non-covalent interactions promote assembly of the supramolecular nanofibers and ultimately determine the bulk physical properties of the macroscopic gels. In this study, we use oscillatory rheology, Fourier-transform infrared spectroscopy, and circular-dichroism spectroscopy to better understand the assembly mechanism of a typical PA molecule known as PA-1. Self-assembly of PA-1 is triggered by counterion screening and stabilized by van der Waals and hydrophobic forces, ionic bridging, and coordination and hydrogen bonding. The concentration, electronic structure, and hydration of counterions significantly influence self-assembly and gel mechanical properties.
AB - Peptide amphiphile molecules (PAs) developed in our laboratory self-assemble from aqueous media into three-dimensional networks of bioactive nanofibers. Multiple non-covalent interactions promote assembly of the supramolecular nanofibers and ultimately determine the bulk physical properties of the macroscopic gels. In this study, we use oscillatory rheology, Fourier-transform infrared spectroscopy, and circular-dichroism spectroscopy to better understand the assembly mechanism of a typical PA molecule known as PA-1. Self-assembly of PA-1 is triggered by counterion screening and stabilized by van der Waals and hydrophobic forces, ionic bridging, and coordination and hydrogen bonding. The concentration, electronic structure, and hydration of counterions significantly influence self-assembly and gel mechanical properties.
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UR - http://www.scopus.com/inward/citedby.url?scp=33644885444&partnerID=8YFLogxK
U2 - 10.1002/adfm.200500161
DO - 10.1002/adfm.200500161
M3 - Article
AN - SCOPUS:33644885444
VL - 16
SP - 499
EP - 508
JO - Advanced Functional Materials
JF - Advanced Functional Materials
SN - 1616-301X
IS - 4
ER -