Affiliation
National Centre for Biomedical Engineering Science, National University of Ireland, Galway, Republic of Ireland.Issue Date
2008-10-21MeSH
Achilles TendonAnimals
Biocompatible Materials
Calorimetry, Differential Scanning
Cattle
Cell Survival
Chemistry, Physical
Collagen
Cross-Linking Reagents
Dendrimers
Microscopy, Electron, Scanning
Ninhydrin
Peptides
Polyamines
Protein Structure, Tertiary
Spectroscopy, Fourier Transform Infrared
Metadata
Show full item recordCitation
Enhancing amine terminals in an amine-deprived collagen matrix. 2008, 24 (20):11752-61 LangmuirPublisher
ACS PublicationsJournal
Langmuir : the ACS journal of surfaces and colloidsDOI
10.1021/la801913cPubMed ID
18774827Additional Links
http://pubs.acs.org/doi/abs/10.1021/la801913cAbstract
Collagen, though widely used as a core biomaterial in many clinical applications, is often limited by its rapid degradability which prevents full exploitation of its potential in vivo. Polyamidoamine (PAMAM) dendrimer, a highly branched macromolecule, possesses versatile multiterminal amine surface groups that enable them to be tethered to collagen molecules and enhance their potential. In this study, we hypothesized that incorporation of PAMAM dendrimer in a collagen matrix through cross-linking will result in a durable, cross-linked collagen biomaterial with free -NH 2 groups available for further multi-biomolecular tethering. The aim of this study was to assess the physicochemical properties of a G1 PAMAM cross-linked collagen matrix and its cellular sustainability in vitro. Different amounts of G1 PAMAM dendrimer (5 or 10 mg) were integrated into bovine-derived collagen matrices through a cross-linking process, mediated by 5 or 25 mM 1-ethyl-3-(3-dimethylaminopropyl) carbodiimide (EDC) in 5 mM N-hydroxysuccinimide (NHS) and 50 mM 2-morpholinoethane sulfonic acid buffer at pH 5.5. The physicochemical properties of resultant matrices were investigated with scanning electron microscopy (SEM), collagenase degradation assay, differential scanning calorimetry (DSC), Fourier transform infrared (FTIR) spectra, and ninhydrin assay. Cellular sustainability of the matrices was assessed with Alamar Blue assay and SEM. There was no significant difference in cellular behavior between the treated and nontreated groups. However, the benefit of incorporating PAMAM in the cross-linking reaction was limited when higher concentrations of either agent were used. These results confirm the hypothesis that PAMAM dendrimer can be incorporated in the collagen cross-linking process in order to modulate the properties of the resulting cross-linked collagen biomaterial with free -NH 2 groups available for multi-biomolecular tethering.Item Type
ArticleLanguage
enISSN
0743-7463ae974a485f413a2113503eed53cd6c53
10.1021/la801913c
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