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Related Concept Videos

Fibril-associated Collagen01:11

Fibril-associated Collagen

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Fibril-associated collagens are a type of collagens present in the extracellular matrix with interrupted triple helices or FACIT (Fibril-associated collagens interrupted triple-helices). FACIT help connect and attach the collagen fibrils with each other as well as with other proteins of the extracellular matrix.
For example, the type II collagen fibrils in cartilage have covalently bound type IX fibril-associated collagens at regular intervals. Other types of fibril-associated collagens are...
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A Biomimetic Model for Liver Cancer to Study Tumor-Stroma Interactions in a 3D Environment with Tunable Bio-Physical Properties
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Molecular level evaluation on HEMA interaction with a collagen model.

Noriko Hiraishi1, Naoya Tochio2, Takanori Kigawa3

  • 1Cariology and Operative Dentistry, Department of Oral Health Sciences, Graduate School, Tokyo Medical and Dental University, 1-5-45 Yushima, Bunkyo-ku, Tokyo 113-8549, Japan.

Dental Materials : Official Publication of the Academy of Dental Materials
|December 16, 2014
PubMed
Summary

2-Hydroxyethylmethacrylate (HEMA) does not bind to collagen in dentin, contrary to its role in dental adhesion. Saturation transfer difference NMR confirmed no molecular interaction, suggesting water layers on collagen prevent direct HEMA binding.

Keywords:
2-ydroxyethylmethacrylateAtelocollagenDental adhesivesDentinNuclear magnetic resonance

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Area of Science:

  • Biomaterials Science
  • Dental Materials
  • Biophysical Chemistry

Background:

  • 2-Hydroxyethylmethacrylate (HEMA) is a key monomer in dental adhesives, known to diffuse into dentin.
  • Its proposed mechanism involves interaction with collagen to promote adhesion.
  • Understanding this interaction at a molecular level is crucial for optimizing dental bonding agents.

Purpose of the Study:

  • To investigate the molecular-level interaction between HEMA and collagen.
  • To elucidate the binding mechanism of HEMA to dentin collagen using advanced spectroscopic techniques.

Main Methods:

  • Preliminary assessment of HEMA binding to demineralized human dentin powder using spectrophotometry.
  • Detailed molecular interaction study using atelocollagen as a collagen model.
  • Saturation Transfer Difference Nuclear Magnetic Resonance (STD-NMR) spectroscopy.

Main Results:

  • Spectrophotometric analysis showed no change in HEMA concentration, indicating no binding to dentin collagen.
  • STD-NMR experiments revealed no saturation transfer from atelocollagen to HEMA.
  • Absence of STD signals confirmed no direct molecular interaction between HEMA and atelocollagen.

Conclusions:

  • HEMA does not directly interact with collagen at the molecular level.
  • The collagen fibrils in dentin may be shielded by water molecules at the dentin-adhesive interface.
  • This hydration layer likely prevents direct HEMA binding, challenging current adhesion models.