Enhancing amine terminals in an amine-deprived collagen matrix.
Tiong, William H C Damodaran, Gopinath Naik, Hemantkumar Kelly, John L Pandit, Abhay
Tiong, William H C
Damodaran, Gopinath
Naik, Hemantkumar
Kelly, John L
Pandit, Abhay
Advisors
Editors
Other Contributors
Date
2008-10-21
Date Submitted
Keywords
Other Subjects
Subject 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
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
Planned Date
Start Date
Collaborators
Principal Investigators
Alternative Titles
Publisher
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.
Language
en
ISSN
0743-7463
eISSN
ISBN
DOI
10.1021/la801913c
PMID
18774827