Three new water-stable aqueous dioxidovanadium(V) complexes, [(VVO2L1–3)M(H2O)n] (1–3), incorporating hydrazone ligands with different alkali metals (Na+/K+) as counterions were synthesized and characterized by various physicochemical approaches, including single-crystal X-ray diffraction (SCXRD). Time-dependent spectroscopic/spectrometric techniques were used to determine their aqueous-phase stabilities. Blood compatibility studies were employed to investigate their efficacy and stability with human red blood cells. Lipophilicity and calf thymus (CT)–DNA interaction of 1–3 were investigated using conventional techniques. High-resolution molecular structures of the adduct formed between 1 and hen egg white lysozyme (HEWL) were determined by SCXRD. The structural analysis reveals that the compound self-assembles within protein crystals, forming a dimeric structure that non-covalently interacts with the protein surface. The binding of 1 to HEWL was also evaluated through different spectroscopic methods. Fluorescence data indicate that 1 can also bind the physiologically relevant protein human serum albumin at pH 7.4. Furthermore, the cytotoxicity of 1–3 was evaluated against the lung (A549) and human breast adenocarcinoma (MCF-7) cancer cell lines, as well as an human embryonic kidney cell line (HEK-293) noncancerous cell line. 1 (IC50 value of 9.2 ± 0.1 μM) is more effective than the other two complexes. It induces cell death via apoptosis.
Binding of Aqueous-Stable, Lipophilic, Hemocompatible Anticancer V V O 2 Metallodrugs with Biological Molecules: X-ray Structures of the Adduct of the V V –hydrazonato Complex with Hen Egg White Lysozyme / Mohapatra, Deepika; Pattanayak, Pratikshya Das; Kaminsky, Werner; Paolillo, Maddalena; Tito, Gabriella; Ferraro, Giarita; Merlino, Antonello; Dinda, Rupam. - In: INORGANIC CHEMISTRY. - ISSN 0020-1669. - 65:12(2026), pp. 6412-6433. [10.1021/acs.inorgchem.5c05201]
Binding of Aqueous-Stable, Lipophilic, Hemocompatible Anticancer V V O 2 Metallodrugs with Biological Molecules: X-ray Structures of the Adduct of the V V –hydrazonato Complex with Hen Egg White Lysozyme
Paolillo, Maddalena;Tito, Gabriella;Ferraro, Giarita;Merlino, Antonello;
2026
Abstract
Three new water-stable aqueous dioxidovanadium(V) complexes, [(VVO2L1–3)M(H2O)n] (1–3), incorporating hydrazone ligands with different alkali metals (Na+/K+) as counterions were synthesized and characterized by various physicochemical approaches, including single-crystal X-ray diffraction (SCXRD). Time-dependent spectroscopic/spectrometric techniques were used to determine their aqueous-phase stabilities. Blood compatibility studies were employed to investigate their efficacy and stability with human red blood cells. Lipophilicity and calf thymus (CT)–DNA interaction of 1–3 were investigated using conventional techniques. High-resolution molecular structures of the adduct formed between 1 and hen egg white lysozyme (HEWL) were determined by SCXRD. The structural analysis reveals that the compound self-assembles within protein crystals, forming a dimeric structure that non-covalently interacts with the protein surface. The binding of 1 to HEWL was also evaluated through different spectroscopic methods. Fluorescence data indicate that 1 can also bind the physiologically relevant protein human serum albumin at pH 7.4. Furthermore, the cytotoxicity of 1–3 was evaluated against the lung (A549) and human breast adenocarcinoma (MCF-7) cancer cell lines, as well as an human embryonic kidney cell line (HEK-293) noncancerous cell line. 1 (IC50 value of 9.2 ± 0.1 μM) is more effective than the other two complexes. It induces cell death via apoptosis.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
