2-Methacryloyloxyethyl N-butylcarbamate: a new co-monomer for synthesis of polyurethane hydrogels with improved mechanical properties for biomedical applications

Hydrogels with tunable hydrophilic and mechanical properties were synthesized by the free radical polymerization of 2-hydroxyethyl methacrylate (HEMA) and 2-methacryloyloxyethyl N-butylcarbamate. The resulting hydrogels were investigated for their equilibrium water content, sessile drop water contac...

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Bibliographic Details
Published in:Journal of biomaterials science. Polymer ed. 2005-01, Vol.16 (10), p.1303-1318
Main Authors: Mequanint, K., Sheardown, H.
Format: Article
Language:English
Subjects:
2-HYDROXYETHYL METHACRYLATE (HEMA)
2-METHACRYLOYLOXYETHYL N-BUTYLCARBAMATE (MBC)
Calorimetry, Differential Scanning
HYDROGEL
Hydrogels - chemical synthesis
MECHANICAL PROPERTIES
Polyhydroxyethyl Methacrylate - chemistry
Polyurethanes - chemical synthesis
PROTEIN ADSORPTION
Spectroscopy, Fourier Transform Infrared
Tensile Strength
Urethane - analogs & derivatives
Urethane - chemistry
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Summary:Hydrogels with tunable hydrophilic and mechanical properties were synthesized by the free radical polymerization of 2-hydroxyethyl methacrylate (HEMA) and 2-methacryloyloxyethyl N-butylcarbamate. The resulting hydrogels were investigated for their equilibrium water content, sessile drop water contact angles, gel fraction, mechanical properties and protein adsorption. Results indicated that co-polymer hydrogels have good hydrophilicity and that, with the incorporation of the 2-methacryloyloxyethyl N-butylcarbamate, mechanical properties could be improved significantly without affecting other important properties. Lysozyme and albumin adsorption experiments demonstrated that, similar to most hydrogel materials, the co-polymer hydrogels adsorb more lysozyme than albumin and that the adsorption was dependent on hydrophilicity. The control poly(HEMA) hydrogels were found to adsorb more protein than the co-polymer hydrogels; this is thought to be primarily a consequence of protein absorption rather than protein adsorption.
ISSN:0920-5063
1568-5624
DOI:10.1163/156856205774269548