Interaction of the anticancer gallium(III) complexes of 8-hydroxyquinoline and maltol with human serum proteins
Gespeichert in:
Verfasser / Beitragende:
[Éva Enyedy, Orsolya Dömötör, Krisztina Bali, Anasztázia Hetényi, Tiziano Tuccinardi, Bernhard Keppler]
Ort, Verlag, Jahr:
2015
Enthalten in:
JBIC Journal of Biological Inorganic Chemistry, 20/1(2015-01-01), 77-88
Format:
Artikel (online)
Online Zugang:
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| 024 | 7 | 0 | |a 10.1007/s00775-014-1211-9 |2 doi |
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| 245 | 0 | 0 | |a Interaction of the anticancer gallium(III) complexes of 8-hydroxyquinoline and maltol with human serum proteins |h [Elektronische Daten] |c [Éva Enyedy, Orsolya Dömötör, Krisztina Bali, Anasztázia Hetényi, Tiziano Tuccinardi, Bernhard Keppler] |
| 520 | 3 | |a Tris(8-quinolinolato)gallium(III) (KP46) and tris(maltolato)gallium(III) (GaM) are promising orally active antitumor metallodrugs currently undergoing clinical trials. Their interaction with human serum albumin (HSA) and transferrin (Tf) was studied in detail in aqueous solution by the combination of various methods such as spectrofluorometry, UV-vis spectrophotometry, 1H and saturation transfer difference NMR spectroscopy, and ultrafiltration-UV-vis spectrophotometry. Binding data were evaluated quantitatively. Tf was found to replace the original ligand much less efficiently in KP46 than in GaM, whereas a significant noncovalent binding of KP46 with HSA (log K′=4.04) retaining the coordination environment around gallium(III) was found. The interaction between HSA and KP46 was also confirmed by protein-complex modeling calculations. On the basis of the conditional stability constants, the distribution of gallium(III) in serum was computed and compared for these metallodrugs under physiological conditions, and revealed the prominent role of HSA in the case of KP46 and that of Tf for GaM. Graphical abstract: | |
| 540 | |a SBIC, 2014 | ||
| 690 | 7 | |a Solution equilibrium |2 nationallicence | |
| 690 | 7 | |a Albumin |2 nationallicence | |
| 690 | 7 | |a Transferrin |2 nationallicence | |
| 690 | 7 | |a Binding affinity |2 nationallicence | |
| 690 | 7 | |a Fluorescence |2 nationallicence | |
| 690 | 7 | |a apoTf : Apotransferrin |2 nationallicence | |
| 690 | 7 | |a GaM : Tris(3-hydroxy-2-methyl-4H-pyran-4-onato)gallium(III) |2 nationallicence | |
| 690 | 7 | |a HEPES : 4-(2-Hydroxyethyl)-1-piperazineethanesulfonic acid |2 nationallicence | |
| 690 | 7 | |a HMM : High molecular mass |2 nationallicence | |
| 690 | 7 | |a HSA : Human serum albumin |2 nationallicence | |
| 690 | 7 | |a HQ : 8-Hydroxyquinoline |2 nationallicence | |
| 690 | 7 | |a KP46 : Tris(8-quinolinolato)gallium(III) |2 nationallicence | |
| 690 | 7 | |a LMM : Low molecular mass |2 nationallicence | |
| 690 | 7 | |a PDB : Protein Data Bank |2 nationallicence | |
| 690 | 7 | |a STD : Saturation transfer difference |2 nationallicence | |
| 690 | 7 | |a Tf : Human serum transferrin |2 nationallicence | |
| 700 | 1 | |a Enyedy |D Éva |u Department of Inorganic and Analytical Chemistry, University of Szeged, Dóm tér 7, 6720, Szeged, Hungary |4 aut | |
| 700 | 1 | |a Dömötör |D Orsolya |u Department of Inorganic and Analytical Chemistry, University of Szeged, Dóm tér 7, 6720, Szeged, Hungary |4 aut | |
| 700 | 1 | |a Bali |D Krisztina |u Department of Inorganic and Analytical Chemistry, University of Szeged, Dóm tér 7, 6720, Szeged, Hungary |4 aut | |
| 700 | 1 | |a Hetényi |D Anasztázia |u Department of Medical Chemistry, University of Szeged, Dóm tér 8, 6720, Szeged, Hungary |4 aut | |
| 700 | 1 | |a Tuccinardi |D Tiziano |u Department of Pharmacy, University of Pisa, 56126, Pisa, Italy |4 aut | |
| 700 | 1 | |a Keppler |D Bernhard |u Institute of Inorganic Chemistry, University of Vienna, Waehringer Str. 42, 1090, Vienna, Austria |4 aut | |
| 773 | 0 | |t JBIC Journal of Biological Inorganic Chemistry |d Springer Berlin Heidelberg |g 20/1(2015-01-01), 77-88 |x 0949-8257 |q 20:1<77 |1 2015 |2 20 |o 775 | |
| 856 | 4 | 0 | |u https://doi.org/10.1007/s00775-014-1211-9 |q text/html |z Onlinezugriff via DOI |
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| 950 | |B NATIONALLICENCE |P 856 |E 40 |u https://doi.org/10.1007/s00775-014-1211-9 |q text/html |z Onlinezugriff via DOI | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Enyedy |D Éva |u Department of Inorganic and Analytical Chemistry, University of Szeged, Dóm tér 7, 6720, Szeged, Hungary |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Dömötör |D Orsolya |u Department of Inorganic and Analytical Chemistry, University of Szeged, Dóm tér 7, 6720, Szeged, Hungary |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Bali |D Krisztina |u Department of Inorganic and Analytical Chemistry, University of Szeged, Dóm tér 7, 6720, Szeged, Hungary |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Hetényi |D Anasztázia |u Department of Medical Chemistry, University of Szeged, Dóm tér 8, 6720, Szeged, Hungary |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Tuccinardi |D Tiziano |u Department of Pharmacy, University of Pisa, 56126, Pisa, Italy |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Keppler |D Bernhard |u Institute of Inorganic Chemistry, University of Vienna, Waehringer Str. 42, 1090, Vienna, Austria |4 aut | ||
| 950 | |B NATIONALLICENCE |P 773 |E 0- |t JBIC Journal of Biological Inorganic Chemistry |d Springer Berlin Heidelberg |g 20/1(2015-01-01), 77-88 |x 0949-8257 |q 20:1<77 |1 2015 |2 20 |o 775 | ||