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Biomaterials2004; 25(14); 2831-2841; doi: 10.1016/j.biomaterials.2003.09.066

Influence of different collagen species on physico-chemical properties of crosslinked collagen matrices.

Abstract: Collagen-based scaffolds are appealing products for the repair of cartilage defects using tissue engineering strategies. The present study investigated the species-related differences of collagen scaffolds with and without 1-ethyl-3-(3-dimethyl aminopropyl) carbodiimide (EDC)/N-hydroxysuccinimide (NHS)-crosslinking. Resistance against collagenase digestion, swelling ratio, amino acid sequence, shrinkage temperature, ultrastructural matrix morphology, crosslinking density and stress-strain characteristics were determined to evaluate the physico-chemical properties of equine- and bovine-collagen-based scaffolds. Three-factor ANOVA analysis revealed a highly significant effect of collagen type (p=0.0001), crosslinking (p=0.0001) and time (p=0.0001) on degradation of the collagen samples by collagenase treatment. Crosslinked equine collagen samples showed a significantly reduced swelling ratio compared to bovine collagen samples (p< 0.0001). The amino acid composition of equine collagen revealed a higher amount of hydroxylysine and lysine. Shrinkage temperatures of non-crosslinked samples showed a significant difference between equine (60 degrees C) and bovine collagen (57 degrees C). Three-factor ANOVA analysis revealed a highly significant effect of collagen type (p=0.0001), crosslinking (p=0.0001) and matrix condition (p=0.0001) on rupture strength measured by stress-strain analysis. The ultrastructure, the crosslinking density and the strain at rupture between collagen matrices of both species showed no significant differences. For tissue engineering purposes, the higher enzymatic stability, the higher form stability, as well as the lower risk of transmissible disease make the case for considering equine-based collagen. This study also indicates that results obtained for scaffolds based on a certain collagen species may not be transferable to scaffolds based on another, because of the differing physico-chemical properties.
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Publication Date: 2004-02-14 PubMed ID: 14962561DOI: 10.1016/j.biomaterials.2003.09.066Google Scholar: Lookup
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  • Comparative Study
  • Evaluation Study
  • Journal Article
  • Research Support
  • Non-U.S. Gov't
  • Research Support
  • U.S. Gov't
  • P.H.S.

Summary

This research summary has been generated with artificial intelligence and may contain errors and omissions. Refer to the original study to confirm details provided. Submit correction.

The research article explores the differences between collagen scaffolds derived from equine (horse) and bovine (cow) sources. It presents findings on how these differences affect the scaffolds’ physical and chemical properties, with potential implications for their use in tissue engineering.

Methodology

  • In this study, researchers compared the properties of collagen scaffolds based on two different species: equine and bovine.
  • The collagen scaffolds were either non-crosslinked or crosslinked with 1-ethyl-3-(3-dimethyl aminopropyl) carbodiimide (EDC) / N-hydroxysuccinimide (NHS). Crosslinking is a process that connects two different polymer chains, in this case collagen, to form a complex that can hold its shape better.
  • The researchers examined multiple properties of the scaffolds, including their resistance against collagenase digestion, swelling ratio, amino acid sequence, shrinkage temperature, matrix morphology, crosslinking density, and stress-strain characteristics.

Findings

  • The analysis showed that collagen type, crosslinking, and time significantly affected the degradation of the collagen samples when treated with collagenase, an enzyme that breaks down collagen.
  • The study found that equine collagen samples that were crosslinked displayed a significantly lower swelling ratio compared to similar bovine collagen samples.
  • The amino acid composition of equine collagen had more hydroxylysine and lysine compared to bovine collagen.
  • The shrinkage temperatures, which is the temperature at which a material starts to shrink, differed between equine (60 degrees C) and bovine collagen (57 degrees C) in non-crosslinked samples.
  • The collagen type, crosslinking, and matrix condition significantly impacted the rupture strength of the collagen matrices, as measured by stress-strain analysis.
  • There were no significant differences in the ultrastructure, or the fine details of a structure visible only with great magnification, and the crosslinking density, or the amount of crosslinks per unit volume, between the equine and bovine collagen matrices. Similarly, there were no significant differences in the strain at rupture between the two types of collagen matrices.

Implications

  • Given their higher enzymatic stability and form stability, and lower risk of transmitting disease, the researchers suggest that equine-based collagen could be more suitable for tissue engineering applications.
  • The study’s results also underline that findings for collagen scaffolds derived from one species may not necessarily apply to scaffolds from another species, due to differences in their physical and chemical properties.

Cite This Article

APA
Angele P, Abke J, Kujat R, Faltermeier H, Schumann D, Nerlich M, Kinner B, Englert C, Ruszczak Z, Mehrl R, Mueller R. (2004). Influence of different collagen species on physico-chemical properties of crosslinked collagen matrices. Biomaterials, 25(14), 2831-2841. https://doi.org/10.1016/j.biomaterials.2003.09.066

Publication

Biomaterials
ISSN: 0142-9612
NlmUniqueID: 8100316
Country: Netherlands
Language: English
Volume: 25
Issue: 14
Pages: 2831-2841

Researcher Affiliations

Angele, Peter
  • Department of Trauma Surgery, University Hospital Regensburg, Franz-Josef-Strauss-Allee 11, Regensburg 93051, Germany. angelepeter@aol.com
Abke, Jochen
    Kujat, Richard
      Faltermeier, Hubert
        Schumann, Detlef
          Nerlich, Michael
            Kinner, Bernd
              Englert, Carsten
                Ruszczak, Zbigniew
                  Mehrl, Robert
                    Mueller, Rainer

                      MeSH Terms

                      • Animals
                      • Cattle
                      • Collagen Type I / chemistry
                      • Collagen Type I / ultrastructure
                      • Collagenases / chemistry
                      • Cross-Linking Reagents / chemistry
                      • Elasticity
                      • Ethyldimethylaminopropyl Carbodiimide / chemistry
                      • Horses
                      • Protein Conformation
                      • Species Specificity
                      • Succinimides / chemistry
                      • Tensile Strength

                      Grant Funding

                      • 1 R01 AR-48132-01 / NIAMS NIH HHS

                      Citations

                      This article has been cited 76 times.
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