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Enhanced proteolytic degradation of molecularly engineered PEG hydrogels in response to MMP-1 and MMP-2.
Journal article

Enhanced proteolytic degradation of molecularly engineered PEG hydrogels in response to MMP-1 and MMP-2.

  • Patterson J Institute for Bioengineering, Ecole Polytechnique Fédérale de Lausanne (EPFL), Lausanne, Switzerland.
  • Hubbell JA
  • 2010-07-30
Published in:
  • Biomaterials. - 2010
Animals
Aorta
Biocompatible Materials
Cell Proliferation
Cells, Cultured
Chemical Engineering
Chick Embryo
Fibroblasts
Hydrogels
Materials Testing
Matrix Metalloproteinase 1
Matrix Metalloproteinase 2
Mice
Peptides
Polyethylene Glycols
English Bioactive hydrogels formed by Michael-type addition reactions of end-functionalized poly(ethylene glycol) macromers with cysteine-containing peptides have been described as extracellular matrix mimetics and tissue engineering scaffolds. Although these materials have shown favorable behavior in vivo in tissue repair, we sought to develop materials formulations that would be more rapidly responsive to cell-induced enzymatic remodeling. In this study, protease-sensitive peptides that have increased k(cat) values were characterized and evaluated for their effects on gel degradability. Biochemical properties for soluble peptides and hydrogels were examined for matrix metalloproteinase (MMP)-1 and MMP-2. The most efficient peptide substrates in some cases overlap and in other cases differ between the two enzymes tested, and a range of k(cat) values was obtained. For each enzyme, hydrogels formed using the peptides with higher k(cat) values degraded faster than a reference with lower k(cat). Fibroblasts showed increased cell spreading and proliferation when cultured in 3D hydrogels with faster degrading peptides, and more cell invasion from aortic ring segments embedded in the hydrogels was observed. These faster degrading gels should provide matrices that are easier for cells to remodel and lead to increased cellular infiltration and potentially more robust healing in vivo.
Language
  • English
Open access status
closed
Identifiers
Persistent URL
https://sonar.ch/global/documents/150916
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