AffiliationNational Centre for Biomedical Engineering Science, National University of Ireland, Galway, Republic of Ireland.
Calorimetry, Differential Scanning
Microscopy, Electron, Scanning
Protein Structure, Tertiary
Spectroscopy, Fourier Transform Infrared
MetadataShow full item record
CitationEnhancing amine terminals in an amine-deprived collagen matrix. 2008, 24 (20):11752-61 Langmuir
JournalLangmuir : the ACS journal of surfaces and colloids
AbstractCollagen, 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.
- Amine functionalization of cholecyst-derived extracellular matrix with generation 1 PAMAM dendrimer.
- Authors: Chan JC, Burugapalli K, Naik H, Kelly JL, Pandit A
- Issue date: 2008 Feb
- Enhanced biological stability of collagen with incorporation of PAMAM dendrimer.
- Authors: Zhong S, Yung LY
- Issue date: 2009 Oct
- Crosslinked collagen/chitosan matrix for artificial livers.
- Authors: Wang XH, Li DP, Wang WJ, Feng QL, Cui FZ, Xu YX, Song XH, van der Werf M
- Issue date: 2003 Aug
- Heparin-modified dendrimer cross-linked collagen matrices for the delivery of basic fibroblast growth factor (FGF-2).
- Authors: Princz MA, Sheardown H
- Issue date: 2008
- Preparation and characterization of novel physically cross-linked hydrogels composed of poly(vinyl alcohol) and amine-terminated polyamidoamine dendrimer.
- Authors: Wu XY, Huang SW, Zhang JT, Zhuo RX
- Issue date: 2004 Feb 20