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- Title
Monomer-Collagen Interactions Studied by Saturation Transfer Difference NMR.
- Authors
Hiraishi, N.; Tochio, N.; Kigawa, T.; Otsuki, M.; Tagami, J.
- Abstract
Functional monomers in dentin adhesives are involved in wetting dental substrates, demineralization, and the formation of calcium salts. However, the interaction of these monomers with collagen is not understood at a molecular/atomic level. We performed saturation transfer difference (STD) NMR spectroscopy to investigate the binding interaction of 2 functional monomers, 4-methacryloyloxyethyl trimellitate anhydride (4-META) and 10-methacryloyloxydecyl dihydrogenphosphate (MDP), with atelocollagen as a triple-helical peptide model. High STD intensities were detected on the protons in the aliphatic region in MDP, whereas they were not detected for 4-META. The STD results imply that MDP has a relatively stable interaction with the collagen, because of the hydrophobic interactions between the hydrophobic MDP moieties and the hydrophobic collagen surface. This finding indicates that MDP-collagen complexation accounts for stable dentin bonding.
- Subjects
MONOMERS; COLLAGEN; NUCLEAR magnetic resonance; DENTAL bonding; DENTAL adhesives; EPITOPES; CALCIUM salts; ANHYDRIDES; HYDROPHOBIC compounds; DENTIN
- Publication
Journal of Dental Research, 2013, Vol 92, Issue 3, p284
- ISSN
0022-0345
- Publication type
Article
- DOI
10.1177/0022034512474310