Glutaraldehyde as a crosslinking agent for collagen-based biomaterials
The formation of Schiff bases during crosslinking of dermal sheep collagen (DSC) with glutaraldehyde (GA), their stability and their reactivity towards GA was studied. All available free amine groups had reacted with GA to form a Schiff base within 5 min after the start of the reaction under the con...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Olde Damink, L. H. H. [verfasserIn] |
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| Format: |
Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
1995 |
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| Schlagwörter: |
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| Anmerkung: |
© Chapman & Hall 1995 |
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| Übergeordnetes Werk: |
Enthalten in: Journal of materials science / Materials in medicine - Kluwer Academic Publishers, 1990, 6(1995), 8 vom: Aug., Seite 460-472 |
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| Übergeordnetes Werk: |
volume:6 ; year:1995 ; number:8 ; month:08 ; pages:460-472 |
| Links: |
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| DOI / URN: |
10.1007/BF00123371 |
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| Katalog-ID: |
OLC2066785563 |
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| 520 | |a The formation of Schiff bases during crosslinking of dermal sheep collagen (DSC) with glutaraldehyde (GA), their stability and their reactivity towards GA was studied. All available free amine groups had reacted with GA to form a Schiff base within 5 min after the start of the reaction under the conditions studied (0.5% (w/w) GA). Before crosslinks are formed the hydrolysable Schiff bases initially present were stabilized by further reaction with GA molecules. An increase in shrinkage temperature (Ts) from 56°C for non-crosslinked DSC (N-DSC) to 78°C for GA crosslinked DSC (G-DSC) was achieved after crosslinking for 1 h. From the relationship between the free amine group content and the Ts during crosslinking it was concluded that higher GA concentrations and longer reaction times will result in the introduction of pendant-GA-related molecules rather than crosslinks. After 24 h crosslinking an average uptake of 3 GA molecules per reacted amine group was found. No increase in the tensile strength of the materials was observed after crosslinking, which may be a result of formation of crosslinks within the fibres rather than in between fibres. Aligning of the fibres by applying a pre-strain to the samples and subsequent crosslinking yielded materials with an increased tensile strength. | ||
| 650 | 4 | |a Tensile Strength | |
| 650 | 4 | |a Shrinkage | |
| 650 | 4 | |a Glutaraldehyde | |
| 650 | 4 | |a Schiff Base | |
| 650 | 4 | |a Crosslinking Agent | |
| 700 | 1 | |a Dijkstra, P. J. |4 aut | |
| 700 | 1 | |a Van Luyn, M. J. A. |4 aut | |
| 700 | 1 | |a Van Wachem, P. B. |4 aut | |
| 700 | 1 | |a Nieuwenhuis, P. |4 aut | |
| 700 | 1 | |a Feijen, J. |4 aut | |
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10.1007/BF00123371 doi (DE-627)OLC2066785563 (DE-He213)BF00123371-p DE-627 ger DE-627 rakwb eng 610 670 VZ Olde Damink, L. H. H. verfasserin aut Glutaraldehyde as a crosslinking agent for collagen-based biomaterials 1995 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Chapman & Hall 1995 The formation of Schiff bases during crosslinking of dermal sheep collagen (DSC) with glutaraldehyde (GA), their stability and their reactivity towards GA was studied. All available free amine groups had reacted with GA to form a Schiff base within 5 min after the start of the reaction under the conditions studied (0.5% (w/w) GA). Before crosslinks are formed the hydrolysable Schiff bases initially present were stabilized by further reaction with GA molecules. An increase in shrinkage temperature (Ts) from 56°C for non-crosslinked DSC (N-DSC) to 78°C for GA crosslinked DSC (G-DSC) was achieved after crosslinking for 1 h. From the relationship between the free amine group content and the Ts during crosslinking it was concluded that higher GA concentrations and longer reaction times will result in the introduction of pendant-GA-related molecules rather than crosslinks. After 24 h crosslinking an average uptake of 3 GA molecules per reacted amine group was found. No increase in the tensile strength of the materials was observed after crosslinking, which may be a result of formation of crosslinks within the fibres rather than in between fibres. Aligning of the fibres by applying a pre-strain to the samples and subsequent crosslinking yielded materials with an increased tensile strength. Tensile Strength Shrinkage Glutaraldehyde Schiff Base Crosslinking Agent Dijkstra, P. J. aut Van Luyn, M. J. A. aut Van Wachem, P. B. aut Nieuwenhuis, P. aut Feijen, J. aut Enthalten in Journal of materials science / Materials in medicine Kluwer Academic Publishers, 1990 6(1995), 8 vom: Aug., Seite 460-472 (DE-627)130865028 (DE-600)1031752-1 (DE-576)023107537 0957-4530 nnns volume:6 year:1995 number:8 month:08 pages:460-472 https://doi.org/10.1007/BF00123371 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-TEC SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_11 GBV_ILN_21 GBV_ILN_23 GBV_ILN_24 GBV_ILN_32 GBV_ILN_60 GBV_ILN_65 GBV_ILN_70 GBV_ILN_2004 GBV_ILN_2006 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_4012 GBV_ILN_4046 GBV_ILN_4082 GBV_ILN_4125 GBV_ILN_4219 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4323 GBV_ILN_4700 AR 6 1995 8 08 460-472 |
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10.1007/BF00123371 doi (DE-627)OLC2066785563 (DE-He213)BF00123371-p DE-627 ger DE-627 rakwb eng 610 670 VZ Olde Damink, L. H. H. verfasserin aut Glutaraldehyde as a crosslinking agent for collagen-based biomaterials 1995 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Chapman & Hall 1995 The formation of Schiff bases during crosslinking of dermal sheep collagen (DSC) with glutaraldehyde (GA), their stability and their reactivity towards GA was studied. All available free amine groups had reacted with GA to form a Schiff base within 5 min after the start of the reaction under the conditions studied (0.5% (w/w) GA). Before crosslinks are formed the hydrolysable Schiff bases initially present were stabilized by further reaction with GA molecules. An increase in shrinkage temperature (Ts) from 56°C for non-crosslinked DSC (N-DSC) to 78°C for GA crosslinked DSC (G-DSC) was achieved after crosslinking for 1 h. From the relationship between the free amine group content and the Ts during crosslinking it was concluded that higher GA concentrations and longer reaction times will result in the introduction of pendant-GA-related molecules rather than crosslinks. After 24 h crosslinking an average uptake of 3 GA molecules per reacted amine group was found. No increase in the tensile strength of the materials was observed after crosslinking, which may be a result of formation of crosslinks within the fibres rather than in between fibres. Aligning of the fibres by applying a pre-strain to the samples and subsequent crosslinking yielded materials with an increased tensile strength. Tensile Strength Shrinkage Glutaraldehyde Schiff Base Crosslinking Agent Dijkstra, P. J. aut Van Luyn, M. J. A. aut Van Wachem, P. B. aut Nieuwenhuis, P. aut Feijen, J. aut Enthalten in Journal of materials science / Materials in medicine Kluwer Academic Publishers, 1990 6(1995), 8 vom: Aug., Seite 460-472 (DE-627)130865028 (DE-600)1031752-1 (DE-576)023107537 0957-4530 nnns volume:6 year:1995 number:8 month:08 pages:460-472 https://doi.org/10.1007/BF00123371 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-TEC SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_11 GBV_ILN_21 GBV_ILN_23 GBV_ILN_24 GBV_ILN_32 GBV_ILN_60 GBV_ILN_65 GBV_ILN_70 GBV_ILN_2004 GBV_ILN_2006 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_4012 GBV_ILN_4046 GBV_ILN_4082 GBV_ILN_4125 GBV_ILN_4219 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4323 GBV_ILN_4700 AR 6 1995 8 08 460-472 |
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10.1007/BF00123371 doi (DE-627)OLC2066785563 (DE-He213)BF00123371-p DE-627 ger DE-627 rakwb eng 610 670 VZ Olde Damink, L. H. H. verfasserin aut Glutaraldehyde as a crosslinking agent for collagen-based biomaterials 1995 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Chapman & Hall 1995 The formation of Schiff bases during crosslinking of dermal sheep collagen (DSC) with glutaraldehyde (GA), their stability and their reactivity towards GA was studied. All available free amine groups had reacted with GA to form a Schiff base within 5 min after the start of the reaction under the conditions studied (0.5% (w/w) GA). Before crosslinks are formed the hydrolysable Schiff bases initially present were stabilized by further reaction with GA molecules. An increase in shrinkage temperature (Ts) from 56°C for non-crosslinked DSC (N-DSC) to 78°C for GA crosslinked DSC (G-DSC) was achieved after crosslinking for 1 h. From the relationship between the free amine group content and the Ts during crosslinking it was concluded that higher GA concentrations and longer reaction times will result in the introduction of pendant-GA-related molecules rather than crosslinks. After 24 h crosslinking an average uptake of 3 GA molecules per reacted amine group was found. No increase in the tensile strength of the materials was observed after crosslinking, which may be a result of formation of crosslinks within the fibres rather than in between fibres. Aligning of the fibres by applying a pre-strain to the samples and subsequent crosslinking yielded materials with an increased tensile strength. Tensile Strength Shrinkage Glutaraldehyde Schiff Base Crosslinking Agent Dijkstra, P. J. aut Van Luyn, M. J. A. aut Van Wachem, P. B. aut Nieuwenhuis, P. aut Feijen, J. aut Enthalten in Journal of materials science / Materials in medicine Kluwer Academic Publishers, 1990 6(1995), 8 vom: Aug., Seite 460-472 (DE-627)130865028 (DE-600)1031752-1 (DE-576)023107537 0957-4530 nnns volume:6 year:1995 number:8 month:08 pages:460-472 https://doi.org/10.1007/BF00123371 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-TEC SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_11 GBV_ILN_21 GBV_ILN_23 GBV_ILN_24 GBV_ILN_32 GBV_ILN_60 GBV_ILN_65 GBV_ILN_70 GBV_ILN_2004 GBV_ILN_2006 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_4012 GBV_ILN_4046 GBV_ILN_4082 GBV_ILN_4125 GBV_ILN_4219 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4323 GBV_ILN_4700 AR 6 1995 8 08 460-472 |
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10.1007/BF00123371 doi (DE-627)OLC2066785563 (DE-He213)BF00123371-p DE-627 ger DE-627 rakwb eng 610 670 VZ Olde Damink, L. H. H. verfasserin aut Glutaraldehyde as a crosslinking agent for collagen-based biomaterials 1995 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Chapman & Hall 1995 The formation of Schiff bases during crosslinking of dermal sheep collagen (DSC) with glutaraldehyde (GA), their stability and their reactivity towards GA was studied. All available free amine groups had reacted with GA to form a Schiff base within 5 min after the start of the reaction under the conditions studied (0.5% (w/w) GA). Before crosslinks are formed the hydrolysable Schiff bases initially present were stabilized by further reaction with GA molecules. An increase in shrinkage temperature (Ts) from 56°C for non-crosslinked DSC (N-DSC) to 78°C for GA crosslinked DSC (G-DSC) was achieved after crosslinking for 1 h. From the relationship between the free amine group content and the Ts during crosslinking it was concluded that higher GA concentrations and longer reaction times will result in the introduction of pendant-GA-related molecules rather than crosslinks. After 24 h crosslinking an average uptake of 3 GA molecules per reacted amine group was found. No increase in the tensile strength of the materials was observed after crosslinking, which may be a result of formation of crosslinks within the fibres rather than in between fibres. Aligning of the fibres by applying a pre-strain to the samples and subsequent crosslinking yielded materials with an increased tensile strength. Tensile Strength Shrinkage Glutaraldehyde Schiff Base Crosslinking Agent Dijkstra, P. J. aut Van Luyn, M. J. A. aut Van Wachem, P. B. aut Nieuwenhuis, P. aut Feijen, J. aut Enthalten in Journal of materials science / Materials in medicine Kluwer Academic Publishers, 1990 6(1995), 8 vom: Aug., Seite 460-472 (DE-627)130865028 (DE-600)1031752-1 (DE-576)023107537 0957-4530 nnns volume:6 year:1995 number:8 month:08 pages:460-472 https://doi.org/10.1007/BF00123371 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-TEC SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_11 GBV_ILN_21 GBV_ILN_23 GBV_ILN_24 GBV_ILN_32 GBV_ILN_60 GBV_ILN_65 GBV_ILN_70 GBV_ILN_2004 GBV_ILN_2006 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_4012 GBV_ILN_4046 GBV_ILN_4082 GBV_ILN_4125 GBV_ILN_4219 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4323 GBV_ILN_4700 AR 6 1995 8 08 460-472 |
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10.1007/BF00123371 doi (DE-627)OLC2066785563 (DE-He213)BF00123371-p DE-627 ger DE-627 rakwb eng 610 670 VZ Olde Damink, L. H. H. verfasserin aut Glutaraldehyde as a crosslinking agent for collagen-based biomaterials 1995 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Chapman & Hall 1995 The formation of Schiff bases during crosslinking of dermal sheep collagen (DSC) with glutaraldehyde (GA), their stability and their reactivity towards GA was studied. All available free amine groups had reacted with GA to form a Schiff base within 5 min after the start of the reaction under the conditions studied (0.5% (w/w) GA). Before crosslinks are formed the hydrolysable Schiff bases initially present were stabilized by further reaction with GA molecules. An increase in shrinkage temperature (Ts) from 56°C for non-crosslinked DSC (N-DSC) to 78°C for GA crosslinked DSC (G-DSC) was achieved after crosslinking for 1 h. From the relationship between the free amine group content and the Ts during crosslinking it was concluded that higher GA concentrations and longer reaction times will result in the introduction of pendant-GA-related molecules rather than crosslinks. After 24 h crosslinking an average uptake of 3 GA molecules per reacted amine group was found. No increase in the tensile strength of the materials was observed after crosslinking, which may be a result of formation of crosslinks within the fibres rather than in between fibres. Aligning of the fibres by applying a pre-strain to the samples and subsequent crosslinking yielded materials with an increased tensile strength. Tensile Strength Shrinkage Glutaraldehyde Schiff Base Crosslinking Agent Dijkstra, P. J. aut Van Luyn, M. J. A. aut Van Wachem, P. B. aut Nieuwenhuis, P. aut Feijen, J. aut Enthalten in Journal of materials science / Materials in medicine Kluwer Academic Publishers, 1990 6(1995), 8 vom: Aug., Seite 460-472 (DE-627)130865028 (DE-600)1031752-1 (DE-576)023107537 0957-4530 nnns volume:6 year:1995 number:8 month:08 pages:460-472 https://doi.org/10.1007/BF00123371 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-TEC SSG-OLC-PHA SSG-OLC-DE-84 GBV_ILN_11 GBV_ILN_21 GBV_ILN_23 GBV_ILN_24 GBV_ILN_32 GBV_ILN_60 GBV_ILN_65 GBV_ILN_70 GBV_ILN_2004 GBV_ILN_2006 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_4012 GBV_ILN_4046 GBV_ILN_4082 GBV_ILN_4125 GBV_ILN_4219 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4323 GBV_ILN_4700 AR 6 1995 8 08 460-472 |
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Glutaraldehyde as a crosslinking agent for collagen-based biomaterials |
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The formation of Schiff bases during crosslinking of dermal sheep collagen (DSC) with glutaraldehyde (GA), their stability and their reactivity towards GA was studied. All available free amine groups had reacted with GA to form a Schiff base within 5 min after the start of the reaction under the conditions studied (0.5% (w/w) GA). Before crosslinks are formed the hydrolysable Schiff bases initially present were stabilized by further reaction with GA molecules. An increase in shrinkage temperature (Ts) from 56°C for non-crosslinked DSC (N-DSC) to 78°C for GA crosslinked DSC (G-DSC) was achieved after crosslinking for 1 h. From the relationship between the free amine group content and the Ts during crosslinking it was concluded that higher GA concentrations and longer reaction times will result in the introduction of pendant-GA-related molecules rather than crosslinks. After 24 h crosslinking an average uptake of 3 GA molecules per reacted amine group was found. No increase in the tensile strength of the materials was observed after crosslinking, which may be a result of formation of crosslinks within the fibres rather than in between fibres. Aligning of the fibres by applying a pre-strain to the samples and subsequent crosslinking yielded materials with an increased tensile strength. © Chapman & Hall 1995 |
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The formation of Schiff bases during crosslinking of dermal sheep collagen (DSC) with glutaraldehyde (GA), their stability and their reactivity towards GA was studied. All available free amine groups had reacted with GA to form a Schiff base within 5 min after the start of the reaction under the conditions studied (0.5% (w/w) GA). Before crosslinks are formed the hydrolysable Schiff bases initially present were stabilized by further reaction with GA molecules. An increase in shrinkage temperature (Ts) from 56°C for non-crosslinked DSC (N-DSC) to 78°C for GA crosslinked DSC (G-DSC) was achieved after crosslinking for 1 h. From the relationship between the free amine group content and the Ts during crosslinking it was concluded that higher GA concentrations and longer reaction times will result in the introduction of pendant-GA-related molecules rather than crosslinks. After 24 h crosslinking an average uptake of 3 GA molecules per reacted amine group was found. No increase in the tensile strength of the materials was observed after crosslinking, which may be a result of formation of crosslinks within the fibres rather than in between fibres. Aligning of the fibres by applying a pre-strain to the samples and subsequent crosslinking yielded materials with an increased tensile strength. © Chapman & Hall 1995 |
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The formation of Schiff bases during crosslinking of dermal sheep collagen (DSC) with glutaraldehyde (GA), their stability and their reactivity towards GA was studied. All available free amine groups had reacted with GA to form a Schiff base within 5 min after the start of the reaction under the conditions studied (0.5% (w/w) GA). Before crosslinks are formed the hydrolysable Schiff bases initially present were stabilized by further reaction with GA molecules. An increase in shrinkage temperature (Ts) from 56°C for non-crosslinked DSC (N-DSC) to 78°C for GA crosslinked DSC (G-DSC) was achieved after crosslinking for 1 h. From the relationship between the free amine group content and the Ts during crosslinking it was concluded that higher GA concentrations and longer reaction times will result in the introduction of pendant-GA-related molecules rather than crosslinks. After 24 h crosslinking an average uptake of 3 GA molecules per reacted amine group was found. No increase in the tensile strength of the materials was observed after crosslinking, which may be a result of formation of crosslinks within the fibres rather than in between fibres. Aligning of the fibres by applying a pre-strain to the samples and subsequent crosslinking yielded materials with an increased tensile strength. © Chapman & Hall 1995 |
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