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.
| Original language | English |
|---|---|
| Pages (from-to) | 2624-2631 |
| Number of pages | 8 |
| Journal | Soft Matter |
| Volume | 7 |
| Issue number | 6 |
| DOIs | |
| State | Published - 21 Mar 2011 |
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Effects of chain length on oligopeptide hydrogelation. / Taraban, Marc B.; Ramachandran, Sivakumar; Gryczynski, Ignacy; Gryczynski, Zygmunt; Trewhella, Jill; Yu, Yihua Bruce.
In: Soft Matter, Vol. 7, No. 6, 21.03.2011, p. 2624-2631.Research output: Contribution to journal › Article
TY - JOUR
T1 - Effects of chain length on oligopeptide hydrogelation
AU - Taraban, Marc B.
AU - Ramachandran, Sivakumar
AU - Gryczynski, Ignacy
AU - Gryczynski, Zygmunt
AU - Trewhella, Jill
AU - Yu, Yihua Bruce
PY - 2011/3/21
Y1 - 2011/3/21
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=79952375523&partnerID=8YFLogxK
U2 - 10.1039/c0sm00919a
DO - 10.1039/c0sm00919a
M3 - Article
AN - SCOPUS:79952375523
VL - 7
SP - 2624
EP - 2631
JO - Soft Matter
JF - Soft Matter
SN - 1744-683X
IS - 6
ER -