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Related Experiment Video

Updated: Jun 17, 2026

Determining the Reactivity and Titre of Serum using a Haemagglutination Assay

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Published on: January 29, 2010

HEMA reactivity with demineralized dentin.

Patrick Sharrock¹, Geneviève Grégoire

¹Medical and Spatial Imaging Laboratory, University Toulouse III, Toulouse, France.

Journal of Dentistry

|December 29, 2009

Summary

2-Hydroxyethylmethacrylate (HEMA) does not react with lysine, unlike its analogue glycidoxypropylmethacrylate (GMA). HEMA is retained in demineralized dentine, suggesting solvation within the collagen network.

Area of Science:

Biomaterials Science
Polymer Chemistry
Dental Materials

Background:

Collagen, a key protein in connective tissues, possesses reactive amino groups.
2-Hydroxyethylmethacrylate (HEMA) is a common monomer in dental adhesives.
Glycidoxypropylmethacrylate (GMA) is an epoxy analogue of HEMA with potential for different reactivity.

Purpose of the Study:

To compare the reactivity of HEMA and GMA with lysine, an amino acid found in collagen.
To determine if HEMA can chemically bond with collagen fibers.
To investigate the interaction of HEMA with demineralized dentine.

Main Methods:

Capillary electrophoresis to analyze reaction products.
Computer-aided chemistry for reaction analysis.

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Infrared spectroscopy to assess HEMA retention in demineralized dentine.

Main Results:

HEMA did not form new molecular species upon contact with lysine.
GMA completely reacted with lysine, forming the expected addition product.
Infrared spectroscopy revealed strong affinity and retention of HEMA in demineralized dentine, even after extensive washing.

Conclusions:

HEMA does not chemically react with the amino groups of lysine.
The retention of HEMA in demineralized dentine suggests solvation within the collagen polymer network.
This finding has implications for the understanding of HEMA-based dental adhesive interactions with dentine.