Enhancing amine terminals in an amine-deprived collagen matrix.

Hdl Handle:
http://hdl.handle.net/10147/144010
Title:
Enhancing amine terminals in an amine-deprived collagen matrix.
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.
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
Issue Date:
21-Oct-2008
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
Description:
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.
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
ISSN:
0743-7463

Full metadata record

DC FieldValue Language
dc.contributor.authorTiong, William H Cen
dc.contributor.authorDamodaran, Gopinathen
dc.contributor.authorNaik, Hemantkumaren
dc.contributor.authorKelly, John Len
dc.contributor.authorPandit, Abhayen
dc.date.accessioned2011-10-05T13:02:18Z-
dc.date.available2011-10-05T13:02:18Z-
dc.date.issued2008-10-21-
dc.identifier.citationEnhancing amine terminals in an amine-deprived collagen matrix. 2008, 24 (20):11752-61 Langmuiren
dc.identifier.issn0743-7463-
dc.identifier.pmid18774827-
dc.identifier.doi10.1021/la801913c-
dc.identifier.urihttp://hdl.handle.net/10147/144010-
dc.descriptionCollagen, 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.en
dc.description.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.-
dc.language.isoenen
dc.publisherACS Publicationsen
dc.relation.urlhttp://pubs.acs.org/doi/abs/10.1021/la801913cen
dc.subject.meshAchilles Tendon-
dc.subject.meshAnimals-
dc.subject.meshBiocompatible Materials-
dc.subject.meshCalorimetry, Differential Scanning-
dc.subject.meshCattle-
dc.subject.meshCell Survival-
dc.subject.meshChemistry, Physical-
dc.subject.meshCollagen-
dc.subject.meshCross-Linking Reagents-
dc.subject.meshDendrimers-
dc.subject.meshMicroscopy, Electron, Scanning-
dc.subject.meshNinhydrin-
dc.subject.meshPeptides-
dc.subject.meshPolyamines-
dc.subject.meshProtein Structure, Tertiary-
dc.subject.meshSpectroscopy, Fourier Transform Infrared-
dc.titleEnhancing amine terminals in an amine-deprived collagen matrix.en
dc.typeArticleen
dc.contributor.departmentNational Centre for Biomedical Engineering Science, National University of Ireland, Galway, Republic of Ireland.en
dc.identifier.journalLangmuir : the ACS journal of surfaces and colloidsen
dc.description.provinceConnacht-
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