Abstract

Human serum transferrin (hTf) is a principal protein that binds to and transports Ti(IV) in blood, so the Ti(IV)–transferrin complex (Ti2–hTf) is studied in this work with an electrochemical method. While the direct electrochemistry of the complex is achieved after being embedded in a polyethyleneimine (PEI) film, thus a pair of stable, well-defined and quasi-reversible cyclic volammetric peaks can be observed with the formal potential at −639mV (vs. SCE), the role of reduction of Ti(IV) in trafficking of Ti(IV) by human serum transferrin is also discussed based on the experimental results that Ti2–hTf undergoes a proton-coupled one electron transfer reaction and Ti(IV)–transferrin is reduced to Ti(III)–transferrin under a mildly acidic condition. This work may provide more information about the transport of titanium in vivo.

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