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site I and negative carbonyl groups may slightly interact with
positively charged residues such as Lys-195, Lys-199, Arg-218,
Arg-222, His-242, and Arg-257 which are located at the entrance
of the site I cavity.
The molecular docking has been employed to further under-
stand precisely the binding site of the Pt4+ compound and HSA.
HSA comprises of three homologous domains (I–III): I (residues
1–195), II (196–383), III (384–585), each domain comprises of
subdomains that posses common structural motifs. The principal
regions of ligand binding to HSA are located in hydrophobic
cavities of subdomains IIA and IIIA, which are consistent with
Sudlow sites I and II, respectively. In the present study, Autodock
program is applied to calculate the possible conformation of the
Pt4+ compound that binds to the protein. Fig. 8C shows that the
Pt4+ compound more favorably fits in the cavity of subdomains IIA,
which corresponds to site I. His-288, Glu-153, Arg-257, Gln-196,
Glu-292 and Arg-222 of site I were around the 4 Å of the
compound, of which Arg-257, Arg-222 and His-288 may be involved
in the electrostatic interaction.
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In this paper, a potential anti-hepatoma drug cis,cis,trans-
[Pt(NH3)2Cl2(O2CCH2CH2COOH)-(OCONHC16H33)] was synthe-
sized and it showed excellent anti-liver cancer activity. The
interaction of human serum albumin and the compound was
investigated employing different spectroscopic and molecular
docking techniques. The results revealed that the secondary
structure of protein was affected upon interaction with the
compound. Fluorescence results indicated the presence of the
static quenching mechanism in the binding of the Pt4+ com-
pound to the protein. Based on spectral data we have concluded
that the Pt4+ compound bound to site I of protein, which is
located in the hydrophobic pocket of subdomain IIA.
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Cancer Biother. Radiopharm., 2012, 27, 452–456.
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Acknowledgements
This work was supported by grants from Medical and Techno-
logic Development Project of Shandong province (2011QZ028).
The authors thank Dr Yamin Chang for his technical support in
Pt4+ compound synthesis and Dr James. H. Haywood of Michigan
State University for editing the manuscript.
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