Self-Assembly of Peptide−Amphiphile Nanofibers:  The Roles of Hydrogen Bonding and Amphiphilic Packing

Sergey E. Paramonov, Ho-Wook Jun, and Jeffrey D. Hartgerink*
Contribution from the Departments of Chemistry and Bioengineering, Rice University, 6100 Main Street, MS60, Houston, Texas 77005
J. Am. Chem. Soc., 2006, 128 (22), pp 7291–7298
DOI: 10.1021/ja060573x
Publication Date (Web): May 16, 2006
Copyright © 2006 American Chemical Society
*

In papers with more than one author, the asterisk indicates the name of the author to whom inquiries about the paper should be addressed.

, jdh@rice.edu

Abstract

Abstract Image

The role of hydrogen bonding and amphiphilic packing in the self-assembly of peptide−amphiphiles (PAs) was investigated using a series of 26 PA derivatives, including 19 N-methylated variants and 7 alanine mutants. These were studied by circular dichroism spectroscopy, a variety of Fourier transform infrared spectroscopies, rheology, and vitreous ice cryo-transmission electron microscopy. From these studies, we have been able to determine which amino acids are critical for the self-assembly of PAs into nanofibers, why the nanofiber is favored over other possible nanostructures, the orientation of hydrogen bonding with respect to the nanofiber axis, and the constraints placed upon the portion of the peptide most intimately associated with the biological environment. Furthermore, by selectively eliminating key hydrogen bonds, we are able to completely change the nanostructure resulting from self-assembly in addition to modifying the macroscopic mechanical properties associated with the assembled gel. This study helps to clarify the mechanism of self-assembly for peptide amphiphiles and will thereby help in the design of future generations of PAs.

View: Full Text HTML | Hi-Res PDF

Tools

History

  • Published In Issue June 07, 2006
  • Received January 25, 2006
    Revised Manuscript Received April 7, 2006

Recommend & Share

Related Content

Other ACS content by these authors: