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      Titanium and Protein Adsorption: An Overview of Mechanisms and Effects of Surface Features

      review-article
      * ,
      Materials
      MDPI
      titanium, protein adsorption, biomaterials, surface modifications, cell interactions

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          Abstract

          Titanium and its alloys, specially Ti6Al4V, are among the most employed materials in orthopedic and dental implants. Cells response and osseointegration of implant devices are strongly dependent on the body–biomaterial interface zone. This interface is mainly defined by proteins: They adsorb immediately after implantation from blood and biological fluids, forming a layer on implant surfaces. Therefore, it is of utmost importance to understand which features of biomaterials surfaces influence formation of the protein layer and how to guide it. In this paper, relevant literature of the last 15 years about protein adsorption on titanium-based materials is reviewed. How the surface characteristics affect protein adsorption is investigated, aiming to provide an as comprehensive a picture as possible of adsorption mechanisms and type of chemical bonding with the surface, as well as of the characterization techniques effectively applied to model and real implant surfaces. Surface free energy, charge, microroughness, and hydroxylation degree have been found to be the main surface parameters to affect the amount of adsorbed proteins. On the other hand, the conformation of adsorbed proteins is mainly dictated by the protein structure, surface topography at the nano-scale, and exposed functional groups. Protein adsorption on titanium surfaces still needs further clarification, in particular concerning adsorption from complex protein solutions. In addition, characterization techniques to investigate and compare the different aspects of protein adsorption on different surfaces (in terms of roughness and chemistry) shall be developed.

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          Most cited references240

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          A review of the biological response to ionic dissolution products from bioactive glasses and glass-ceramics.

          Several inorganic materials such as special compositions of silicate glasses, glass-ceramics and calcium phosphates have been shown to be bioactive and resorbable and to exhibit appropriate mechanical properties which make them suitable for bone tissue engineering applications. However, the exact mechanism of interaction between the ionic dissolution products of such inorganic materials and human cells are not fully understood, which has prompted considerable research work in the biomaterials community during the last decade. This review comprehensively covers literature reports which have investigated specifically the effect of dissolution products of silicate bioactive glasses and glass-ceramics in relation to osteogenesis and angiogenesis. Particularly, recent advances made in fabricating dense biomaterials and scaffolds doped with trace elements (e.g. Zn, Sr, Mg, and Cu) and investigations on the effect of these elements on the scaffold biological performance are summarized and discussed in detail. Clearly, the biological response to artificial materials depends on many parameters such as chemical composition, topography, porosity and grain size. This review, however, focuses only on the ion release kinetics of the materials and the specific effect of the released ionic dissolution products on human cell behaviour, providing also a scope for future investigations and identifying specific research needs to advance the field. The biological performance of pure and doped silicate glasses, phosphate based glasses with novel specific compositions as well as several other silicate based compounds are discussed in detail. Cells investigated in the reviewed articles include human osteoblastic and osteoclastic cells as well as endothelial cells and stem cells. Copyright © 2011 Elsevier Ltd. All rights reserved.
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            Understanding protein adsorption phenomena at solid surfaces.

            Protein adsorption at solid surfaces plays a key role in many natural processes and has therefore promoted a widespread interest in many research areas. Despite considerable progress in this field there are still widely differing and even contradictive opinions on how to explain the frequently observed phenomena such as structural rearrangements, cooperative adsorption, overshooting adsorption kinetics, or protein aggregation. In this review recent achievements and new perspectives on protein adsorption processes are comprehensively discussed. The main focus is put on commonly postulated mechanistic aspects and their translation into mathematical concepts and model descriptions. Relevant experimental and computational strategies to practically approach the field of protein adsorption mechanisms and their impact on current successes are outlined. Copyright © 2011 Elsevier B.V. All rights reserved.
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              Structure and reactivity of water at biomaterial surfaces.

              Molecular self association in liquids is a physical process that can dominate cohesion (interfacial tension) and miscibility. In water, self association is a powerful organizational force leading to a three-dimensional hydrogen-bonded network (water structure). Localized perturbations in the chemical potential of water as by, for example, contact with a solid surface, induces compensating changes in water structure that can be sensed tens of nanometers from the point of origin using the surface force apparatus (SFA) and ancillary techniques. These instruments reveal attractive or repulsive forces between opposing surfaces immersed in water, over and above that anticipated by continuum theory (DLVO), that are attributed to a variable density (partial molar volume) of a more-or-less ordered water structure, depending on the water wettability (surface energy) of the water-contacting surfaces. Water structure at surfaces is thus found to be a manifestation of hydrophobicity and, while mechanistic/theoretical interpretation of experimental results remain the subject of some debate in the literature, convergence of experimental observations permit, for the first time, quantitative definition of the relative terms 'hydrophobic' and 'hydrophilic'. In particular, long-range attractive forces are detected only between surfaces exhibiting a water contact angle theta > 65 degrees (herein defined as hydrophobic surfaces with pure water adhesion tension tau O = gamma O cos theta 30 dyn/cm). These findings suggest at least two distinct kinds of water structure and reactivity: a relatively less-dense water region against hydrophobic surfaces with an open hydrogen-bonded network and a relatively more-dense water region against hydrophilic surfaces with a collapsed hydrogen-bonded network. Importantly, membrane and SFA studies reveal a discrimination between biologically-important ions that preferentially solubilizes divalent ions in more-dense water regions relative to less-dense water regions in which monovalent ions are enriched. Thus, the compelling conclusion to be drawn from the collective scientific evidence gleaned from over a century of experimental and theoretical investigation is that solvent properties of water within the interphase separating a solid surface from bulk water solution vary with contacting surface chemistry. This interphase can extend tens of nanometers from a water-contacting surface due to a propagation of differences in self association between vicinal water and bulk-phase water. Physicochemical properties of interfacial water profoundly influence the biological response to materials in a surprisingly straightforward manner when key measures of biological activity sensitive to interfacial phenomena are scaled against water adhesion tension tau O of contacting surfaces. As examples, hydrophobic surfaces (tau O 30 dyn/cm) do not support adsorption because this mechanism is energetically unfavorable. Protein-adsorbing hydrophobic surfaces are inefficient contact activators of the blood coagulation cascade whereas protein-repellent hydrophilic surfaces are efficient activators of blood coagulation. Mammalian cell attachment is a process distinct from protein adsorption that occurs efficiently to hydrophilic surfaces but inefficiently to hydrophobic surfaces. (ABSTRACT TRUNCATED)
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                Author and article information

                Contributors
                Role: Academic Editor
                Journal
                Materials (Basel)
                Materials (Basel)
                materials
                Materials
                MDPI
                1996-1944
                24 March 2021
                April 2021
                : 14
                : 7
                : 1590
                Affiliations
                Department of Applied Science and Technology, Politecnico di Torino, 10129 Turin, Italy; silvia.spriano@ 123456polito.it
                Author notes
                [* ]Correspondence: jacopo.barberi@ 123456polito.it ; Tel.: +39-011-0904567
                Author information
                https://orcid.org/0000-0002-9649-5401
                https://orcid.org/0000-0002-7367-9777
                Article
                materials-14-01590
                10.3390/ma14071590
                8037091
                33805137
                93c2e3d3-fe73-4d88-b1bb-ac4b866654a2
                © 2021 by the authors.

                Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license ( http://creativecommons.org/licenses/by/4.0/).

                History
                : 05 February 2021
                : 19 March 2021
                Categories
                Review

                titanium,protein adsorption,biomaterials,surface modifications,cell interactions

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