These authors contributed equally to this work.
Nanostructures from the self-assembly of α-helical peptide amphiphiles
Version of Record online: 30 JAN 2014
Copyright © 2014 European Peptide Society and John Wiley & Sons, Ltd.
Journal of Peptide Science
Volume 20, Issue 3, pages 223–228, March 2014
How to Cite
Meng, Q., Kou, Y., Ma, X., Guo, L. and Liu, K. (2014), Nanostructures from the self-assembly of α-helical peptide amphiphiles. J. Peptide Sci., 20: 223–228. doi: 10.1002/psc.2606
- Issue online: 11 FEB 2014
- Version of Record online: 30 JAN 2014
- Manuscript Accepted: 26 NOV 2013
- Manuscript Revised: 19 NOV 2013
- Manuscript Received: 15 SEP 2013
- National Natural Science Foundation of China. Grant Number: 81202465 and 81373266
- National Key Technologies R & D Program for New Drugs of China. Grant Number: 2012ZX09301003
- peptide amphiphiles;
Self-assembly of PAs composed of palmitic acid and several repeated heptad peptide sequences, C15H31CO-(IEEYTKK)n-NH2 (n = 1–4, represented by PA1–PA4), was investigated systematically. The secondary structures of the PAs were characterized by CD. PA3 and PA4 (n = 3 and 4, respectively) showed an α-helical structure, whereas PA1 and PA2 (n = 1 and 2, respectively) did not display an α-helical conformations under the tested conditions. The morphology of the self-assembled peptides in aqueous medium was studied by transmission electron microscopy. As the number of heptad repeats in the PAs increased, the nanostructure of the self-assembled peptides changed from nanofibers to nanovesicles. Changes of the secondary structures and the self-assembly morphologies of PA3 and PA4 in aqueous medium with various cations were also studied. The critical micelle concentrations were determined using a pyrene fluorescence probe. In conclusion, this method may be used to design new peptide nanomaterials. Copyright © 2014 European Peptide Society and John Wiley & Sons, Ltd.