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Biodistribution of anti‐diabetic Zn(II) complexes in human serum and in vitro protein‐binding studies by means of CZE–ICP‐MS
Author(s) -
Bytzek Anna K.,
Enyedy Éva A.,
Kiss Tamás,
Keppler Bernhard K.,
Hartinger Christian G.
Publication year - 2009
Publication title -
electrophoresis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.666
H-Index - 158
eISSN - 1522-2683
pISSN - 0173-0835
DOI - 10.1002/elps.200900212
Subject(s) - biodistribution , chemistry , in vitro , blood proteins , human insulin , pharmacology , plasma protein binding , drug , in vivo , insulin , biochemistry , medicine , biology , microbiology and biotechnology
Application of modern analytical technology for studying the fate of metallodrugs after administration to the blood is of utmost importance for drug development. Zn(II) compounds are under development as insulin‐enhancing drugs with potential use in the treatment of diabetes. In comparison to the well‐established vanadium compounds, especially the lower risk of adverse effects due to the essentiality of the element in biological processes is advantageous. Herein, CZE–ICP‐MS studies on the interaction of Zn(II)‐maltolato, ‐2‐picolinato and ‐2,6‐dipicolinato complexes with human serum proteins are discussed and modeling calculations were confirmed by experimental results. Studies with human serum reveal preference for HSA over other less abundant proteins and serum components.