Binding of V(IV) to human transferrin: potential relevance to anticancer activity of vanadocene dichloride.
The action mechanism of vanadocene dichloride, Cp2VCl2 (Cp=eta5-C5H5), has been investigated by interaction with human serum transferrin for its promising antitumor activities. Our results have shown that Cp2VCl2 binds to transferrin and form a new complex, and the calculated apparent association constant is 1.37 x 10(5)M(-1) from the fluorescence quenching. Simultaneously, the variation of the secondary structure of transferrin occurs, most probably due to the coordination of the amino residues of protein with VIV. It was evidenced that Cp is released free in solution after VIV binding to transferrin by 1H NMR measurements. These results have shown that Cp2VCl2 forms a complex with transferrin, which may provide a possible pathway in the transport and targeted delivery of the antitumor agent.
Du
Hongyan
H
Beijing National Laboratory for Molecular Sciences, State Key Laboratory for Structural Chemistry of Unstable and Stable Species, Center for Molecular Sciences, Institute of Chemistry, Chinese Academy of Sciences, Beijing 100080, China.
Xiang
Junfeng
J
Zhang
Yazhou
Y
Tang
Yalin
Y
Xu
Guangzhi
G
D000970:Antineoplastic Agents / Q000494:pharmacology*; D001059:Apoproteins / Q000378:metabolism*; D006801:Humans; D019906:Nuclear Magnetic Resonance, Biomolecular; D013050:Spectrometry, Fluorescence; D013056:Spectrophotometry, Ultraviolet; D014168:Transferrin / Q000378:metabolism*; D014639:Vanadium / Q000378:metabolism*; D017968:Vanadium Compounds / Q000494:pharmacology*