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Matrix-assisted laser desorption ionization mass spectrometry: a new tool for probing interactions between proteins and metal surfaces. Use in dental implantology.

作者信息

Leize E M, Leize E J, Leize M C, Voegel J C, Van Dorsselaer A

机构信息

UMR 7509 CNRS, Université Louis Pasteur, 1 rue Blaise Pascal, Strasbourg Cedex, 67008, France.

出版信息

Anal Biochem. 1999 Jul 15;272(1):19-25. doi: 10.1006/abio.1999.4142.

Abstract

The fixation in the bone of an artificial titanium tooth root is believed to be initiated by the rapid adsorption of the proteins present in the surgical cavity on the titanium surface. The study of this adsorption should make it possible to predict the osseointegration capacities of new implant surface treatments. We describe here a new method, based on matrix-assisted laser desorption ionization-mass spectrometry (MALDI-MS), for quantifying proteins adsorbed on titanium surfaces fully identical to these designed for implantology. The key step of this method is a new MALDI-MS sample preparation allowing the adsorbed proteins to be removed from the surface and to be homogeneously dispersed in the matrix crystals. The adsorption of a model protein (lysozyme) on two titanium surfaces (polished and sandblasted) was studied in order to evaluate the method. The absolute MALDI-MS intensity was shown to vary linearly with the amount of adsorbed lysozyme. After dipping the titanium surfaces for different times in lysozyme solutions at different concentrations, the maximum amount of adsorbed lysozyme was measured by MALDI-MS and was shown to correspond to a lysozyme monolayer, which is consistent with results described in the literature.

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