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Resumo(s)
Polyoxometalates (POMs) biological and biomedical applications have attracted increasing attention over the past decades. Polyoxometalates are inorganic transition metal oxygen clusters characterized by having multiple structures and tunable electronic properties that are well-known to be effective inhibitors of many enzymes, such as ATPases. Herein, a new hybrid POM of the Keggin type, Vanadium-substituted Keggin polyoxotungstate, namely (C₆H₁₅N)₄(C₆H₁₆N)₆(VW₁₂O₄₀)₂⋅4H₂O, was synthesized via wet-chemical methods in aqueous solution. Its purity was confirmed, and the compound was fully characterized by single-crystal X-ray diffraction, infrared spectroscopy, UV–visible spectroscopy, and thermogravimetric analysis. The Keggin-type compound exhibited a half maximal inhibitory concentration (IC50) value of 8.25 μM toward calcium adenosine triphosphatase (Ca2+- ATPase) inhibition, as measured spectrophotometrically using a coupled pyruvate kinase/lactate dehydrogenase enzyme assay. Hirshfeld surface analysis was employed to investigate intermolecular interactions within the crystal structure, revealing differences in hydrogen bonding and oxygen-based contacts. These structural features may suggest a possible relationship with the observed biological activity; however, no direct correlation with Ca2+-ATPase inhibition can be firmly established from the present data. Therefore, the observed relationships should be considered preliminary and structural in nature, rather than mechanistic. Further computational and biological studies are required to clarify the role of these interactions in enzyme inhibition.
Descrição
Palavras-chave
Vanadium substituted Keggin Polyoxometalates Hybrid polyoxometalates Calcium ATPase inhibition Polyoxometalate synthesis Enzyme coupled assay Hirshfeld surface analysis
Contexto Educativo
Citação
Editora
Elsevier