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      Electrostatic control of protein adsorption on UV-photofunctionalized titanium

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          Abstract

          Ultraviolet (UV)-photofunctionalization of titanium to enable the establishment of a nearly complete bone-implant contact was reported recently. However, the underlying mechanism for this is unknown. We hypothesized that UV-treated titanium surfaces acquire distinct electrostatic properties that may play important roles in determining the bioactivity of these surfaces. The objective of this study was to determine the protein adsorption capability of UV-treated titanium surfaces under various electrostatic environments. The amount of albumin adsorbed on UV-treated and untreated titanium disks was evaluated under different pH conditions above and below the isoelectric points of albumin and titanium. The effects of additional treatment with various ionic solutions were also examined. Albumin adsorption on UV-treated surfaces at pH 7.0 was considerably greater (6-fold after 3h of incubation and 2.5-fold after 24h) than that to UV-untreated surfaces. UV-enhanced albumin adsorption was abrogated at pH 3.0 or when these titanium surfaces were treated with anions, while maintaining UV-induced superhydrophilicity. Albumin adsorption on UV-untreated titanium surfaces increased after treating these surfaces with divalent cations but not after treating them with monovalent cations. These results indicated that UV-treated titanium surfaces are electropositively charged as opposed to electronegatively charged UV-untreated titanium surfaces. This distinct UV-induced electrostatic property predominantly regulates the protein adsorption capability of titanium, superseding the effect of hydrophilic status, and converts titanium surfaces from bioinert to bioactive. As a result, direct titanium-protein interactions take place exclusively on UV-treated titanium surfaces without the aid of bridging ions.

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          Author and article information

          Journal
          Acta Biomaterialia
          Acta Biomaterialia
          Elsevier BV
          17427061
          October 2010
          October 2010
          : 6
          : 10
          : 4175-4180
          Article
          10.1016/j.actbio.2010.05.006
          © 2010

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