2008
DOI: 10.1021/ja076364+
|View full text |Cite
|
Sign up to set email alerts
|

Reconsideration of Serum Ti(IV) Transport:  Albumin and Transferrin Trafficking of Ti(IV) and Its Complexes

Abstract: The trafficking of titanium(IV) by human serum transferrin (HsTf) has been implicated in the physiology of this hydrolysis-prone metal. The current work broadens to include the further interactions of Ti(IV) in serum that bear on this model. Ti2HsTf (2 equiv) binds the transferrin receptor TfR1 with Kd1 = 6.3 +/- 0.4 nM and Kd2 = 410 +/- 150 nM, values that are the tightest yet measured for a metal other than iron but weaker than the corresponding ones for Fe2HsTf due to both slightly slower on rates and sligh… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
1

Citation Types

3
103
1
1

Year Published

2009
2009
2017
2017

Publication Types

Select...
4
2

Relationship

1
5

Authors

Journals

citations
Cited by 105 publications
(108 citation statements)
references
References 71 publications
3
103
1
1
Order By: Relevance
“…Binding to SA affords a mechanism by which a Ti(IV) compound, such as the titanocene moiety (22,23), could be delivered intact to cancer cells and directly exhibit its effect. Several hydrolysis-prone Ti(IV) compounds, including the titanocene moiety, importantly, bind to SA (13,20,22,23). However, similar to results with Tf, the addition of SA to cell-viability assays does not improve the cytotoxicity displayed by different Ti(IV) compounds (24), except Titanocene Y (24).…”
mentioning
confidence: 67%
See 4 more Smart Citations
“…Binding to SA affords a mechanism by which a Ti(IV) compound, such as the titanocene moiety (22,23), could be delivered intact to cancer cells and directly exhibit its effect. Several hydrolysis-prone Ti(IV) compounds, including the titanocene moiety, importantly, bind to SA (13,20,22,23). However, similar to results with Tf, the addition of SA to cell-viability assays does not improve the cytotoxicity displayed by different Ti(IV) compounds (24), except Titanocene Y (24).…”
mentioning
confidence: 67%
“…The hydrophobic compound binds with fairly high affinity to SA, however. Ti(IV) citrate (a mixture of species) is able to competitively interact with both proteins, rapidly binding as an ion to Tf and as a Ti(IV) monocitrate complex to SA, likely in a hydrophilic pocket (13). This behavior of Ti(IV) citrate is comparable to that of titanocene dichloride, although the titanocene moiety would be expected to bind in a hydrophobic site in SA (13).…”
Section: Resultsmentioning
confidence: 99%
See 3 more Smart Citations