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Hydration and preferential molecular adsorption on titanium in vitro
Surface sensitive spectroscopies, Auger electron and X-ray photoelectron (XPS), were used to determine changes in titanium oxide composition, oxide stoichiometry and adsorbed surface species as a function of exposure to human serum in a balanced electrolyte (serum/SIE) and 8.0 mM ethylenediaminetetr...
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Published in: | Biomaterials 1992, Vol.13 (8), p.553-561 |
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Main Authors: | , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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Summary: | Surface sensitive spectroscopies, Auger electron and X-ray photoelectron (XPS), were used to determine changes in titanium oxide composition, oxide stoichiometry and adsorbed surface species as a function of exposure to human serum in a balanced electrolyte (serum/SIE) and 8.0 mM ethylenediaminetetraacetic acid in a balanced electrolyte (EDTA/SIE) at 37°C. Before immersion, the oxide was near ideal TiO
2, covered by two types of hydroxyl groups: acidic OH(s) with oxygens doubly coordinated to titanium and basic Ti-OH groups singly coordinated. After extended exposure to both solutions, up to 5000 h (ca. 208 d), the surface concentration of OH groups increased and non-elemental P appeared. The P LVV Auger transition and P 2p spectra indicated the peak positions were similar to reference phosphate compounds. The adsorbed phosphate species were presumed to be either Ti-H
2PO
4 or Ti-HPO
4
−. The XPS data suggested that a lipoprotein and/or glycolipid film was adsorbed to the specimens exposed to serum/SIE. Analysis of the preferential lipoprotein/glycolipid adsorption using electrostatic bonding concepts contributed to the refinement of the hierarchical model for the Ti-tissue interface. The salient features are that Ti metal is not in direct contact with the biological milieu, rather there is a gradual transition from the bulk metal, near-stoichiometric oxide, Ca and P substituted hydrated oxide, adsorbed lipoproteins and glycolipids, proteoglycans, collagen filaments and bundles to cells. |
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ISSN: | 0142-9612 1878-5905 |
DOI: | 10.1016/0142-9612(92)90108-Z |