| Title | Protein matrices for improved wound healing: Elastase inhibition by a synthetic peptide model |
| Publication Type | Journal Article |
| 2010 |
| Authors | Vasconcelos, A, Pêgo, AP, Henriques, L, Lamghari, M, Cavaco-Paulo, A |
| Journal | BiomacromoleculesBiomacromolecules |
| Volume | 11 |
| Issue | 9 |
| Pagination | 2213 - 2220 |
| Date Published | 2010/// |
| 15257797 (ISSN) |
| animal cell, Animals, article, Atomic force microscopy, Biodegradation, Biological degradation, Biological functions, biomaterial, Bombyx, Bowman Birk inhibitor, Bowman-Birk inhibitors, cell proliferation, Chronic wounds, controlled study, Cytotoxicity test, Degradation, Elastase, elastase inhibitor, enzyme activity, Enzyme inhibition, Fibroins, Film composition, In-vitro, keratin, Keratins, mass spectrometry, materials testing, Mice, Microscopy, Atomic Force, NIH 3T3 Cells, nonhuman, pancreatic elastase, Peptide Fragments, Peptides, priority journal, protein binding, Protein matrices, Release rate, Silk, Silk fibroin, Spectrometry, Mass, Electrospray Ionization, Sus, Swine, Synthetic peptide, Trypsin Inhibitor, Bowman-Birk Soybean, Trypsin Inhibitors, wound fluid, Wound healing |
| The unique properties of silk fibroin were combined with keratin to develop new wound-dressing materials. Silk fibroin/keratin (SF/K) films were prepared to reduce high levels of elastase found on chronic wounds. This improved biological function was achieved by the incorporation of a small peptide synthesized based on the reactive-site loop of the Bowman-Birk Inhibitor (BBI) protein. In vitro degradation and release were evaluated using porcine pancreatic elastase (PPE) solution as a model of wound exudate. It was found that biological degradation and release rate are highly dependent on film composition. Furthermore, the level of PPE activity can be tuned by changing the film composition, thus showing an innovative way of controlling the elastase-antielastase imbalance found on chronic wounds. © 2010 American Chemical Society. |
| http://www.scopus.com/inward/record.url?eid=2-s2.0-77956552375&partnerID=40&md5=7d7dc9145b9655d9ba0461eb7a85d118 |
