Electrochemical behavior of Ti/Al2O3 interfaces produced by diffusion bonding

In the field of biomedical applications a special interest exists regarding the study of the physicochemical and mechanical behaviour of materials, with special focus on the electrochemical degradation of metal/ceramic interfaces. In fact, etal/ceramic interfaces may be present in several biomedical devices, ranging from external or implantable sensors, to dental implants. Diffusion bonding represents an important technique since, in opposition to other production technologies, such as active metal brazing, avoid the possible liberation of certain chemical components harmful to health. The aim of this work is to study the electrochemical degradation of the interface formed between commercially pure Ti and Al2O3 produced by diffusion bonding, in contact with a physiological solution. The present approach included the evaluation of the contribution of individual and pairs of interfacial layers on the global degradation processes. For this propose d.c. electrochemical techniques were used to monitor the open-circuit potential, and to perform potentiodynamic polarization and galvanic corrosion evaluation. Also, electrochemical impedance spectroscopy was used as a complementary technique of the corrosion behaviour of the interface. Chemical composition and morphology of samples and corrosion products were evaluated by SEM and EDS analysis. According to experimental results, two principal reaction layers were formed in the interface: TiAl and Ti3Al. The TiAl layer appears to be the responsible for the strong increase in corrosion rate of the interface.Fundação para a Ciência e Tecnologia -POCTI/CTM/33384/2000; SFRH/BPD/ 5518/2001

Cytocompatibility of Medical Biomaterials Containing Nickel by Osteoblasts: a Systematic Literature Review

The present review is based on a survey of 21 studies on the cytocompatibility of medical biomaterials containing nickel, as assessed by cell culture of human and animal osteoblasts or osteoblast-like cells. Among the biomaterials evaluated were stainless steel, NiTi alloys, pure Ni, Ti, and other pure metals. The materials were either commercially available, prepared by the authors, or implanted by various techniques to generate a protective layer of oxides, nitrides, acetylides. The observation that the layers significantly reduced the initial release of metal ions and increased cytocompatibility was confirmed in cell culture experiments. Physical and chemical characterization of the materials was performed. This included, e.g., surface characterization (roughness, wettability, corrosion behavior, quantity of released ions, microhardness, and characterization of passivation layer). Cytocompatibility tests of the materials were conducted in the cultures of human or animal osteoblasts and osteoblast-like cells. The following assays were carried out: cell proliferation and viability test, adhesion test, morphology (by fluorescent microscopy or SEM). Also phenotypic and genotypic markers were investigated. In the majority of works, it was found that the most cytocompatible materials were stainless steel and NiTi alloy. Pure Ni was rendered and less cytocompatible. All the papers confirmed that the consequence of the formation of protective layers was in significant increase of cytocompatibility of the materials. This indicates the possible further modifications of the manufacturing process (formation of the passivation layer)

Characterization of a saporin isoform with lower ribosome-inhibiting activity.

We have expressed in Escherichia coli five isoforms of saporin, a single-chain ribosome-inactivating protein (RIP). Translation inhibition activities of the purified recombinant polypeptides in vitro were compared with those of recombinant dianthin 30, a less potent and closely related RIP, and of ricin A chain. Dianthin 30, and a saporin isoform encoded by a cDNA from leaf tissue (SAP-C), both had about one order of magnitude lower activity in translation inhibition assays than all other isoforms of saporin tested. We recently demonstrated that saporin extracted from seeds of Saponaria officinalis binds to alpha2-macroglobulin receptor (alpha2MR; also termed low density lipoprotein-receptor-related-protein), indicating a general mechanism of interaction of plant RIPs with the alpha2MR system [Cavallaro, Nykjaer, Nielsen and Soria (1995) Eur. J. Biochem. 232, 165-171]. Here we report that SAP-C bound to alpha2MR equally well as native saporin. However, the same isoform had about ten times lower cytotoxicity than the other saporin isoforms towards different cell lines. This indicates that the lower cell-killing ability of the SAP-C isoform is presumably due to its altered interaction with the protein synthesis machinery of target cells. Since saporin binding to the alpha2MR is competed by heparin, we also tested in cell-killing experiments Chinese hamster ovary cell lines defective for expression of either heparan sulphates or proteoglycans. No differences were observed in cytotoxicity using native saporin or the recombinant isoforms. Therefore saporin binding to the cell surface should not be mediated by interaction with proteoglycans, as is the case for other alpha2MR ligands