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Removal of noncollagenous components affects dentin bonding.
P N R Pereira1, A K B Bedran-de-Castro, W R Duarte
1Department of Operative Dentistry, University of North Carolina, Chapel Hill, North Carolina, USA. patricia_pereira@dentistry.unc.edu
Summary
Noncollagenous matrix components in dentin, including chondroitin sulfate glycosaminoglycans and trypsin-digestible proteins, are vital for effective dentin bonding. Their removal compromises collagen fibril structure and reduces bond strength.
Area of Science:
- Biomaterials Science
- Dental Materials
- Biochemistry
Background:
- Fibrillar type I collagen's structural integrity is crucial for dentin bonding.
- Noncollagenous matrix components are closely associated with collagen in dentin.
- Their potential contribution to dentin bonding remains largely unexplored.
Purpose of the Study:
- To investigate the role of noncollagenous matrix components in dentin bonding.
- To determine if chondroitin sulfate glycosaminoglycans and trypsin-digestible proteins influence dentin bond strength.
- To assess the impact of enzymatic treatment on collagen fibril architecture and its relation to bonding.
Main Methods:
- Bovine dentin specimens were acid-etched and treated with chondroitinase ABC (C-ABC), endo-beta-galactosidase (Endo-beta), or trypsin.
- Control groups received no enzymatic treatment.
- All specimens were bonded using One-Step, and bond strengths were analyzed statistically.
- Scanning Electron Microscopy (SEM) was used to evaluate collagen fibril architecture.
Main Results:
- Enzymatic treatment with C-ABC or trypsin significantly decreased bond strengths in rewetted groups (p < 0.05).
- Endo-beta treatment showed no significant effect on bond strengths (p > 0.05).
- SEM analysis revealed significant loss of collagen fibril architecture in C-ABC and trypsin treated groups.
Conclusions:
- Chondroitin sulfate glycosaminoglycans and trypsin-digestible noncollagenous proteins play a role in maintaining the collagen fibril scaffold.
- These components are essential for optimal dentin bonding by preserving the open dimensions of the collagen structure.
- Understanding these interactions can inform the development of improved dental adhesives.