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    Enhancing amine terminals in an amine-deprived collagen matrix.

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    Authors
    Tiong, William H C
    Damodaran, Gopinath
    Naik, Hemantkumar
    Kelly, John L
    Pandit, Abhay
    Affiliation
    National Centre for Biomedical Engineering Science, National University of Ireland, Galway, Republic of Ireland.
    Issue Date
    2008-10-21
    MeSH
    Achilles Tendon
    Animals
    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
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    Citation
    Enhancing amine terminals in an amine-deprived collagen matrix. 2008, 24 (20):11752-61 Langmuir
    Publisher
    ACS Publications
    Journal
    Langmuir : the ACS journal of surfaces and colloids
    URI
    http://hdl.handle.net/10147/144010
    DOI
    10.1021/la801913c
    PubMed ID
    18774827
    Additional Links
    http://pubs.acs.org/doi/abs/10.1021/la801913c
    Abstract
    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
    Article
    Language
    en
    ISSN
    0743-7463
    ae974a485f413a2113503eed53cd6c53
    10.1021/la801913c
    Scopus Count
    Collections
    Galway University Hospitals

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