Editorial: Vanadium biochemistry – highlights from the 13th international vanadium symposium

Vanadium biochemistry continues to attract attention since it sits at the intersection of coordination chemistry, chemical biology, and issues related to health and the environment. In biological and aqueous settings, vanadium compounds can undergo hydrolysis, ligand exchange, and redox reactions (Nunes et al., 2021; Dinda et al., 2025; Crans and Miller, 2025). None of this is surprising among first-row transition metals; however, unique for vanadium is the versatile redox chemistry under physiological conditions, combined with vanadium in the +5 oxidation state being both an excellent structural and an electronic analog of phosphate. These are recurring and distinctive topics across bioinorganic vanadium research that shape mechanistic interpretation in enzyme chemistry, compound design and properties in medicinal studies, and toxicology (Crans et al., 2004; Pessoa et al., 2015; Crans and Miller, 2025).

Vanadium’s broader biochemical relevance stems from its ability to undergo redox processes or interfere with phosphorylation-dependent processes (Crans et al., 2004). Vanadate’s resemblance to phosphate underlies its well-established role as an inhibitor of protein tyrosine phosphatases, while pervanadates offer a window into how vanadium-based chemistry can modulate catalytic cysteine residues in signaling enzymes (Mulholland et al., 2026). Polyoxovanadates have also attracted growing interest for their pharmacological potential, beyond their relevance to fundamental coordination chemistry. Reported biological activities span antidiabetic, antibacterial, antiviral, antiprotozoal, and anticancer effects, motivating continued investigation into their therapeutic applications and their interaction with proteins and membrane receptors (Aureliano et al., 2021).

This Frontiers Research Topic, “Vanadium Biochemistry–Highlights from the 13th International Vanadium Symposium,” was developed in connection with the 13th International Vanadium Symposium (Lisbon, 22–24 November 2023) with contributions from plenary speakers and other participants and aimed to bring together representative advances in vanadium chemistry with direct relevance to chemical biology. Across five contributions, a shared message emerges: mechanistic understanding of vanadium in chemical biology cannot be separated from an understanding of its solution behavior, interfacial interactions, and the experimental conditions under which biology is tested.

Two papers directly address the challenge posed by chemical speciation. Ždrnja et al. examine the concentration-dependent stability and hydrolysis of Keggin- and Wells-Dawson-type polyoxotungstates across pH 2-8 in commonly used buffer systems. They employ ³¹P NMR to quantify speciation trends and to reveal how ionic strength and buffer composition shape stability and hydrolysis pathways as reported previously for other systems (Ždrnja et al.). Their findings emphasize a point that is often overlooked: buffer choice and concentration are not inert variables, particularly in polyoxometalate studies and, by extension, in much of vanadium chemistry.

Garribba’s presents a complementary approach, making the case for electron paramagnetic resonance (EPR) as a selective and mechanistically informative tool for probing vanadium(IV) chemistry. The Perspective details solution transformations and coordination environments in vanadium(IV) chemistry, with emphasis on biologically relevant species and their behavior in the presence of biomolecules such as amino acids, reducing agents, and proteins. Considering the redox activity of vanadium compounds, a method to study vanadium(IV) is critical to understand the mechanisms of vanadium-compound in biological systems (Pessoa, et al., 2015; Dinda et al., 2025). In addition, the Perspective highlights the need for a practical standard for the field: speciation characterization should be treated as essential, not as optional support, whenever biological outcomes are reported.

The next group of contributions examines how metal-oxo clusters engage with biological interfaces, which is relevant to connect physicochemical properties to cellular outcomes (Aureliano et al., 2021; Ždrnja et al.). Pashkovskaya et al. study the interaction of Anderson-Evans-type polyoxometalates with lipid membranes, tracking changes in ζ-potential and liposome size across phospholipid compositions. Their results show that membrane composition, including the presence of negatively charged lipids such as cardiolipin, modulates polyoxometalate binding, and that ionic conditions alter observed interaction signatures. For a class of compounds frequently associated with antimicrobial and antitumor activities (Aureliano et al., 2021) this kind of controlled, quantitative treatment of electrostatics-driven association is particularly valuable.

Paredes-Pérez et al. approach protein-like microenvironments from a different angle. They use guanidinium and spermidinium decavanadates as “biomimetic” salts to probe how the anion engages motifs resembling arginine and lysine side chains, which are frequently implicated in the binding of decavanadates to proteins. Through a combination of spectroscopy, crystallography, DFT-derived interaction energies, and non-covalent interaction analyses, they characterize the hydrogen-bonding and electrostatic contacts that explain how polyoxidovanadates can be accommodated within protein environments. The contribution is notable for bridging the gap between a reactive anion in solution and a binding interaction with definable non-covalent architecture.

The final original research article in the Topic illustrates a mature, medicinally oriented vanadium study. Levina et al. report the solution behavior and in vitro antiproliferative activity of a mixed-ligand vanadium(V) complex, incorporating the antifungal and antibacterial agent clioquinol, in glioblastoma (T98G) cells. In this study, biological activity is not treated as a standalone endpoint: the authors track stability and speciation in relevant media by UV-Vis and discuss explicitly how ligand dissociation and hydrolysis both complicate and potentially explain observed cellular effects, including in experiments probing iron dependence. The result is a study where bioactivity observations are mechanistically grounded in the species formed under the studied assay conditions. This study furthermore demonstrates that the vanadium-compounds developed for Chagas disease (Scalese et al., 2021) are also active against glioblastoma.

This collection of original research and perspective articles shows three important future trends in the field of Vanadium Biochemistry. Speciation should be treated as a design principle: concentration, ionic strength, and buffer composition can be determinant variables, especially for redox-active vanadium complexes and polyoxometalates. Multi-modal characterization should offer a path from physicochemical characterization to biological context, linking solution-phase spectroscopy (EPR, ³¹P NMR) with interface-sensitive assays (ζ-potential, liposome readouts). And, mechanistic hypotheses should be tested through translational studies, tracking the chemical forms present in biological media and considering speciation-driven elucidations for cellular outcomes.

“Vanadium Biochemistry–Highlights from the 13th International Vanadium Symposium” captures aspects of a growing field, which may reflect a greater focus on experimentally validated chemical entities that exist in the biological milieu and less concern with the formation and application of isolated compounds (Nunes et al., 2021; Dinda et al., 2025). Furthermore, the development and continued exploration of vanadium-containing therapeutics expand previously reported studies not only of conventional ligand-vanadium coordination complexes (Côrte-Real et al., 2026, Levina et al.), but also larger polyoxovanadates. We hope this collection fosters further dialogue between coordination chemistry, spectroscopy, computation, and cellular research, and helps move vanadium chemical biology toward more reproducible, mechanism-grounded science.

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Footnotes

Edited and reviewed by: Sylvia Mary Draper, Trinity College Dublin, Ireland