Binding Models of Copper(II) Thiosemicarbazone Complexes with Human Serum Albumin: A Speciation Study
Copper(II) complexes of thiosemicarbazones (TSCs) often exhibit anticancer properties, and their pharmacokinetic behavior can be affected by their interaction with blood transport proteins. Interaction of copper(II) complexes of an {N,N,S} donor α-<i>N</i>-pyridyl TSC (Triapine) and an {...
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| Format: | Article |
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MDPI AG
2021-05-01
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| Series: | Molecules |
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| Online Access: | https://www.mdpi.com/1420-3049/26/9/2711 |
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| author | Nóra V. May Attila Jancsó Éva A. Enyedy |
| author_facet | Nóra V. May Attila Jancsó Éva A. Enyedy |
| author_sort | Nóra V. May |
| collection | DOAJ |
| description | Copper(II) complexes of thiosemicarbazones (TSCs) often exhibit anticancer properties, and their pharmacokinetic behavior can be affected by their interaction with blood transport proteins. Interaction of copper(II) complexes of an {N,N,S} donor α-<i>N</i>-pyridyl TSC (Triapine) and an {O,N,S} donor 2-hydroxybenzaldehyde TSC (STSC) with human serum albumin (HSA) was investigated by UV–visible and electron paramagnetic resonance spectroscopy at physiological pH. Asp-Ala-His-Lys and the monodentate N-methylimidazole were also applied as binding models. Conditional formation constants were determined for the ternary copper(II)-TSC complexes formed with HSA, DAHK, and N-methylimidazole based on the spectral changes of both charge transfer and d-d bands. The neutral N-methylimidazole displays a similar binding affinity to both TSC complexes. The partially negatively charged tetrapeptide binds stronger to the positively charged Triapine complex in comparison to the neutral STSC complex, while the opposite trend was observed for HSA, which demonstrates the limitations of the use of simple ligands to model the protein binding. The studied TSC complexes are able to bind to HSA in a fast process, and the conditional constants suggest that their binding strength is only weak-to-moderate. |
| first_indexed | 2024-03-10T11:41:01Z |
| format | Article |
| id | doaj.art-033bed9e9a9b4123b1ba6e4bbe958e91 |
| institution | Directory Open Access Journal |
| issn | 1420-3049 |
| language | English |
| last_indexed | 2024-03-10T11:41:01Z |
| publishDate | 2021-05-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Molecules |
| spelling | doaj.art-033bed9e9a9b4123b1ba6e4bbe958e912023-11-21T18:26:34ZengMDPI AGMolecules1420-30492021-05-01269271110.3390/molecules26092711Binding Models of Copper(II) Thiosemicarbazone Complexes with Human Serum Albumin: A Speciation StudyNóra V. May0Attila Jancsó1Éva A. Enyedy2Centre for Structural Science, Research Centre for Natural Sciences, Magyar Tudósok Körútja 2, H-1117 Budapest, HungaryDepartment of Inorganic and Analytical Chemistry, Interdisciplinary Excellence Centre, University of Szeged, Dóm tér 7, H-6720 Szeged, HungaryDepartment of Inorganic and Analytical Chemistry, Interdisciplinary Excellence Centre, University of Szeged, Dóm tér 7, H-6720 Szeged, HungaryCopper(II) complexes of thiosemicarbazones (TSCs) often exhibit anticancer properties, and their pharmacokinetic behavior can be affected by their interaction with blood transport proteins. Interaction of copper(II) complexes of an {N,N,S} donor α-<i>N</i>-pyridyl TSC (Triapine) and an {O,N,S} donor 2-hydroxybenzaldehyde TSC (STSC) with human serum albumin (HSA) was investigated by UV–visible and electron paramagnetic resonance spectroscopy at physiological pH. Asp-Ala-His-Lys and the monodentate N-methylimidazole were also applied as binding models. Conditional formation constants were determined for the ternary copper(II)-TSC complexes formed with HSA, DAHK, and N-methylimidazole based on the spectral changes of both charge transfer and d-d bands. The neutral N-methylimidazole displays a similar binding affinity to both TSC complexes. The partially negatively charged tetrapeptide binds stronger to the positively charged Triapine complex in comparison to the neutral STSC complex, while the opposite trend was observed for HSA, which demonstrates the limitations of the use of simple ligands to model the protein binding. The studied TSC complexes are able to bind to HSA in a fast process, and the conditional constants suggest that their binding strength is only weak-to-moderate.https://www.mdpi.com/1420-3049/26/9/2711peptide modelalbumin bindingEPR spectroscopyternary complexes |
| spellingShingle | Nóra V. May Attila Jancsó Éva A. Enyedy Binding Models of Copper(II) Thiosemicarbazone Complexes with Human Serum Albumin: A Speciation Study Molecules peptide model albumin binding EPR spectroscopy ternary complexes |
| title | Binding Models of Copper(II) Thiosemicarbazone Complexes with Human Serum Albumin: A Speciation Study |
| title_full | Binding Models of Copper(II) Thiosemicarbazone Complexes with Human Serum Albumin: A Speciation Study |
| title_fullStr | Binding Models of Copper(II) Thiosemicarbazone Complexes with Human Serum Albumin: A Speciation Study |
| title_full_unstemmed | Binding Models of Copper(II) Thiosemicarbazone Complexes with Human Serum Albumin: A Speciation Study |
| title_short | Binding Models of Copper(II) Thiosemicarbazone Complexes with Human Serum Albumin: A Speciation Study |
| title_sort | binding models of copper ii thiosemicarbazone complexes with human serum albumin a speciation study |
| topic | peptide model albumin binding EPR spectroscopy ternary complexes |
| url | https://www.mdpi.com/1420-3049/26/9/2711 |
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