Enzyme-mediated modification of fibrin for tissue engineering: fibrin formulations with peptides
US7241730B2 · kind B2 · utility
Assignees
Inventors
Key dates
| Filing date | Mar 25, 2002 |
| Grant date | Jul 10, 2007 |
| Priority date | — |
| Expiry date | Dec 24, 2023 |
Classification
- Technology area (CPC C)Chemistry; Metallurgy
- CPC primaryC12N2533/56
- WIPO fieldBiotechnology
- WIPO sectorChemistry
Abstract
Heparin-binding regions of several proteins, such as neural cell adhesion molecule, fibronectin, laminin, midkine, and anti-thrombin III have been shown to promote neurite extension on two-dimensional surfaces. The effect of heparin-binding peptides on neurite extension through three-dimensional matrices was investigated by culturing embryonic chick dorsal root ganglia (DRG) within fibrin gels containing chemically attached heparin-binding peptide (HBP). The length of neurites within fibrin gels containing cross-linked HBP was increased by more than 70% over extension through fibrin gels containing no peptide. The HBP sequence of antithrombin III was incorporated into the fibrin gel as the C-terminal domain of a bidomian, chimeric peptide; the N-terminal second domain of this peptide contained the ∀2-plasmin inhibitor substrate for Factor XIIIa. Factor XIIIa, a transglutaminase, was used to chemically attach the HBP-containing chimeric peptide to the fibrin gels during polymerization. The amount of HBP cross-linked into the fibrin gels was determined, after degradation by plasmin using gel permeation chromatography, to be approximately 8 moles of peptide per mole fibrinogen. A pept…
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