Abstract:
:Hydrogels produced from self-assembling peptides and peptide derivatives are being investigated as synthetic extracellular matrices for defined cell culture substrates and scaffolds for regenerative medicine. In many cases, however, they are less stiff than the tissues and extracellular matrices they are intended to mimic, and they are prone to cohesive failure. We employed native chemical ligation to produce peptide bonds between the termini of fibrillized beta-sheet peptides to increase gel stiffness in a chemically specific manner while maintaining the morphology of the self-assembled fibrils. Polymerization, fibril structure, and mechanical properties were measured by SDS-PAGE, mass spectrometry, TEM, circular dichroism, and oscillating rheometry; and cellular responses to matrix stiffening were investigated in cultures of human umbilical vein endothelial cells (HUVECs). Ligation led to a fivefold increase in storage modulus and a significant enhancement of HUVEC proliferation and expression of CD31 on the surface of the gels. The approach was also orthogonal to the inclusion of unprotected RGD-functionalized self-assembling peptides, which further increased proliferation. This strategy broadens the utility of self-assembled peptide materials for applications that require enhancement or modulation of matrix mechanical properties by providing a chemoselective means for doing so without significantly disrupting the gels' fibrillar structure.
journal_name
Biomaterialsjournal_title
Biomaterialsauthors
Jung JP,Jones JL,Cronier SA,Collier JHdoi
10.1016/j.biomaterials.2008.01.008subject
Has Abstractpub_date
2008-05-01 00:00:00pages
2143-51issue
13eissn
0142-9612issn
1878-5905pii
S0142-9612(08)00034-3journal_volume
29pub_type
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