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Immobilization of a bone and cartilage stimulating peptide to a synthetic bone graft.
- Source :
-
Journal of materials science. Materials in medicine [J Mater Sci Mater Med] 2008 May; Vol. 19 (5), pp. 2145-55. Date of Electronic Publication: 2007 Nov 22. - Publication Year :
- 2008
-
Abstract
- A synthetic peptide fragment of human collagen type I (BCSP-1) was linked to the surface of a commercially available ceramic in an effort to improve the properties of the bone graft substitute to accelerate local healing. BCSP-1 was covalently immobilized on the surface of the ceramic via the linkers 3-aminopropyl-triethoxysilane (APTES) and suberic acid bis-N-hydroxysuccinimide ester (DSS). The chosen chemistry was non-cytotoxic. A rat calvaria cell assay using alkaline phosphatase (ALP) as an osteoblast differentiation marker, showed that modifying the surface of the ceramic was enough to enhance ALP activity, although the total cell population on the surface decreased. A significant increase in ALP activity/cell was noted with serum albumin bound to the surface, however, the BCSP-1 bound surface exhibited an even greater ALP activity that showed a surface concentration dependent trend. An optimal BCSP-1 surface density in the range of 0.87-2.24 nmol/cm2 elicited the maximum ALP activity/cell at day 6 of culture. The peptide bound ceramic generated an ALP activity/cell that was roughly 3-fold higher than the non-modified ceramic and 2-fold higher than the APTES-grafted ceramic.
- Subjects :
- Adsorption
Alkaline Phosphatase metabolism
Animals
Cells, Cultured
Chromatography, High Pressure Liquid
Models, Chemical
Models, Statistical
Propylamines
Rats
Silanes chemistry
Succinimides chemistry
Surface Properties
Bone Transplantation instrumentation
Bone and Bones metabolism
Cartilage metabolism
Peptides chemistry
Subjects
Details
- Language :
- English
- ISSN :
- 0957-4530
- Volume :
- 19
- Issue :
- 5
- Database :
- MEDLINE
- Journal :
- Journal of materials science. Materials in medicine
- Publication Type :
- Academic Journal
- Accession number :
- 18030432
- Full Text :
- https://doi.org/10.1007/s10856-007-3306-0