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Characterization of collagen matrices crosslinked using microbial transglutaminase
Ray-Neng Chen1, Hsiu-O Ho, Ming-Thau Sheu
1Graduate Institute of Pharmaceutical Sciences, College of Pharmacy, Taipei Medical University, 250 Wu-Hsing Street, Taipei 110, Taiwan, ROC.
Biomaterials
|February 3, 2005
Summary
Microbial transglutaminase (MTGase) effectively crosslinks collagen biomaterials, enhancing their strength and stability. This enzymatic method offers a non-cytotoxic alternative for collagen matrix modification.
Area of Science:
- Biomaterials Science
- Biochemistry
- Tissue Engineering
Background:
- Collagen is a crucial biomaterial for tissue regeneration and drug delivery.
- Crosslinking enhances collagen matrix stability and mechanical properties.
- Existing crosslinking methods have limitations, necessitating novel approaches.
Purpose of the Study:
- To investigate microbial transglutaminase (MTGase) as a novel crosslinking agent for collagen matrices.
- To evaluate the impact of MTGase crosslinking on collagen mechanical and thermal properties.
- To assess the biocompatibility of MTGase-crosslinked collagen matrices.
Main Methods:
- Porcine type I collagen matrices were prepared.
- Crosslinking was performed using microbial transglutaminase (MTGase) at varying pH conditions.
- Viscosity, tensile strength, denaturation temperature, and cytotoxicity (MTT assay) were analyzed.
Main Results:
- MTGase demonstrated crosslinking activity, increasing collagen solution viscosity.
- Matrices crosslinked at low pH (3 and 4) exhibited significantly higher tensile strength.
- Denaturation temperatures increased for MTGase-treated matrices, indicating enhanced stability.
- MTT assays confirmed the non-cytotoxic nature of the enzyme-crosslinked matrices.
Conclusions:
- Microbial transglutaminase (MTGase) is a viable enzymatic crosslinking agent for collagen.
- MTGase crosslinking improves mechanical strength and thermal stability of collagen matrices.
- This enzymatic approach offers a safe and effective alternative for collagen biomaterial modification.