Abstract
The influence of amino acid sequence on the secondary structure of peptide amphiphile (PAs) cylindrical micelles and fibers that are self-assembled in solution is studied using molecular dynamics simulations. Simulations for two choices of PAs were performed, starting with structures that have the correct overall shape, but which restructure considerably during the simulation, with one fiber being composed of valine rich PAs and the other of alanine rich PAs. Self-assembly is similar in both simulations, with stable fibers (diameter is 7.7-8 nm) obtained after 40 ns. We find that the valine rich PA fiber has a higher β-sheet population than the alanine rich fiber, and that the number of hydrogen bonds is higher. This behavior of the valine rich fiber is consistent with experimental measurements of higher stiffness, and it shows that stiffness can be varied while still maintaining self-assembly.
| Original language | English (US) |
|---|---|
| Article number | 936 |
| Journal | Journal of Nanoparticle Research |
| Volume | 14 |
| Issue number | 8 |
| DOIs | |
| State | Published - Aug 2012 |
Funding
Acknowledgments This research was supported by the National Science Foundation (grant CHE-1147335), and by the DOE NERC EFRC (DE-SC0000989).
Keywords
- Clusters
- Modeling and simulation
- Molecular dynamics simulation
- Peptide amphiphiles
- Secondary structure
- Storage modulus
- β-Sheet
ASJC Scopus subject areas
- Condensed Matter Physics
- Bioengineering
- Atomic and Molecular Physics, and Optics
- General Chemistry
- General Materials Science
- Modeling and Simulation