Format

Send to

Choose Destination
See comment in PubMed Commons below
Soft Matter. 2011;7(6):2624-2631.

Effects of chain length on oligopeptide hydrogelation.

Author information

1
Fischell Department of Bioengineering, University of Maryland, College Park, MD 20742, USA.

Abstract

The co-assembly of mutually complementary, but self-repulsive oligopeptide pairs into viscoelastic hydrogels has been studied. Oligopeptides of 6, 10, and 14 amino acid residues were used to investigate the effects of peptide chain length on the structural and mechanical properties of the resulting hydrogels. Biophysical characterizations, including dynamic rheometry, small-angle X-ray scattering (SAXS) and fluorescence spectroscopy, were used to investigate hydrogelation at the bulk, fiber, and molecular levels, respectively. Upon mixing, the 10-mer peptides and the 14-mer peptides both form hydrogels while the 6-mer peptides do not. SAXS studies point to morphological similarity of the cross-sections of fibers underlying the 10:10 and 14:14 gels. However, fluorescence spectroscopy data suggest tighter packing of the amino acid side chains in the 10:10 fibers. Consistent with this tighter packing, dynamic rheometry data show that the 10:10 gel has much higher elastic modulus than the 14:14 mer (18 kPa vs. 0.1 kPa). Therefore, from the standpoint of mechanical strength, the optimum peptide chain length for this class of oligopeptide-based hydrogels is around 10 amino acid residues.

PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for Royal Society of Chemistry Icon for PubMed Central
    Loading ...
    Support Center