Journal of Inorganic Biochemistry最新文献

{"title":"Proteomic profiling of parthanatos and the neuroprotective potential of sodium perborate tetrahydrate","authors":"Merve Gulsen Bal Albayrak ,&nbsp;Sevinc Yanar ,&nbsp;Tuğcan Korak ,&nbsp;Gurler Akpinar ,&nbsp;Murat Kasap","doi":"10.1016/j.jinorgbio.2025.112984","DOIUrl":"10.1016/j.jinorgbio.2025.112984","url":null,"abstract":"<div><div>Parthanatos is a caspase-independent form of programmed cell death triggered by PARP-1 overactivation and mitochondrial dysfunction, implicated in neurodegenerative diseases. In this study, we performed a proteomic analysis of SH-SY5Y neuronal cells undergoing parthanatos and evaluated the neuroprotective effects of sodium perborate tetrahydrate (SPT), an inorganic boron-containing compound. LC-MS/MS analysis revealed significant alterations in mitochondrial respiration, DNA repair, and inflammatory signaling pathways. Proteins such as MT-CO2, CYC1, POLR2L, and SLC25A5 -implicated in Parkinson's and Huntington's disease pathways- were found to be dysregulated. SPT pre-treatment led to reduced PARP-1 activation, decreased DNA fragmentation, and improved cell viability. These findings suggest that boron-containing inorganics, as metalloids, can modulate molecular targets involved in neuronal survival. Our study contributes novel experimental evidence on the biochemical effects of boron compounds in neurodegenerative processes, complementing current research in metalloid-biomolecule interactions and supporting their potential utility in therapeutic development for neurodegenerative diseases.</div></div>","PeriodicalId":364,"journal":{"name":"Journal of Inorganic Biochemistry","volume":"271 ","pages":"Article 112984"},"PeriodicalIF":3.8,"publicationDate":"2025-06-26","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144513852","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Cadmium(II) complexes with pyridine/dicarboxylic acid ligands as promising molecules for the treatment of oral candidiasis","authors":"Diana Liz Jimenez ,&nbsp;Débora Taisa Keller da Silva ,&nbsp;Talita da Paz Costa Sauda ,&nbsp;Adriana Araújo de Almeida-Apolonio ,&nbsp;Emanuele P.O. Roque ,&nbsp;Pamella Fukuda de Castilho ,&nbsp;João Víctor de Andrade dos Santos ,&nbsp;Sidnei M. Silva ,&nbsp;Lucas Pizzuti ,&nbsp;Amilcar M. Junior ,&nbsp;Victor M. Deflon ,&nbsp;Kelly Mari Pires de Oliveira ,&nbsp;Gleison Antônio Casagrande","doi":"10.1016/j.jinorgbio.2025.112980","DOIUrl":"10.1016/j.jinorgbio.2025.112980","url":null,"abstract":"<div><div>Overgrowth of <em>Candida</em> spp., known for its strong adhesion to biotic and abiotic surfaces, makes treatment difficult in denture stomatitis. To address this challenge, two novel cadmium(II) complexes containing 2,5-pyridinedicarboxylic acid (H₂L) (complex <strong>1</strong> [Cd(HL)(H₂O)(DMSO)I]₂ and [Cd(HL)(H₂O)(bipy)I] complex <strong>2</strong>), were synthesized and fully characterized by X-ray diffractometry, HRMS-ESI (+) spectrometry, ¹H and ¹³C NMR, FT-IR and elemental analysis. These complexes were evaluated for their antifungal, antibiofilm, hemolytic, and mutagenic properties. The interaction of these complexes with established antifungal agents was also investigated. Both complexes demonstrated remarkable antifungal activity, particularly against <em>C. albicans</em> and <em>C. krusei</em>, with MIC ranging from 62.5 (97.91 μM) to 0.48 (0.75 μM) μg/mL and MFC from 125 (195.82 μM) to 3.80 (5.95 μM) μg/mL. Furthermore, these complexes effectively inhibited <em>C. krusei</em> biofilm formation on prosthetic acrylic resin test specimens, with complex <strong>2</strong> showing superior activity. The complexes also displayed synergistic effects with fluconazole, furthermore, sorbitol assays have shown that cell wall is one of the targets of the tested complexes. Importantly, hemolysis assays indicated that the complexes were non-cytotoxic to human erythrocytes, and mutagenicity assays confirmed their non-mutagenic nature. These findings suggest that the synthesized cadmium(II) complexes, particularly complex <strong>2</strong>, possess significant potential as therapeutic agents for the treatment of denture stomatitis and oral candidiasis in general.</div></div>","PeriodicalId":364,"journal":{"name":"Journal of Inorganic Biochemistry","volume":"271 ","pages":"Article 112980"},"PeriodicalIF":3.8,"publicationDate":"2025-06-26","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144501213","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Near-infrared activation of upconversion platforms for non-redox-dependent release of Pt(II)","authors":"Marc-Ricard Batten ,&nbsp;Josep Antoni Gutiérrez-Orgaz ,&nbsp;Fernando Eduardo Maturi ,&nbsp;Luís Dias Carlos ,&nbsp;Helena Oliveira ,&nbsp;Jordi Hernando ,&nbsp;Fernando Novio ,&nbsp;Antonio Rodríguez-Diéguez ,&nbsp;Mercè Capdevila ,&nbsp;Òscar Palacios ,&nbsp;Pau Bayón","doi":"10.1016/j.jinorgbio.2025.112982","DOIUrl":"10.1016/j.jinorgbio.2025.112982","url":null,"abstract":"<div><div>Upconversion nanoparticles (UCNPs) are a class of interesting nanomaterials with unique multi-photon excitation photoluminescence properties, and they have been intensively explored as novel contrast agents for biomedical imaging and drug delivery. The development of photoinduced drug-release devices has been intensively developed in the last years, specially using UCNPs due to their properties to absorb single-band near infrared (NIR) light and subsequently emit high-energy UV-to-visible light which could photoactivate several prodrugs. Some examples of Pt(II) release have been described, all of them from Pt(IV) complexes taking advantage of the Pt(IV)/(II) redox couple. In this work, NIR light-responsive LiYF₄:Yb/Tm UCNPs are presented as carrier systems to exert photoinduced Pt(II) drug release. For this, the surface of UCNPs were coated with an amphiphilic polymer to convert hydrophobic nanoparticles into hydrophilic and to load novel Pt(II) complexes. It is demonstrated that NIR radiation-induced Pt(II) drug release can be achieved without the need to use the Pt(IV)/(II) redox couple as a trigger. In this way, under NIR excitation, UCNPs can transform NIR irradiation into UV radiation which causes direct Pt(II) drug release in a spatial and temporal control manner. The release process has been monitored in real-time. Two platforms containing two different Pt(II) complexes have been studied, both showing similar results in terms of the enhancement of toxicity caused by the increase in Pt(II) concentration. Furthermore, a significant improvement of cytotoxicity against melanoma A375 cells was observed after irradiation of these platforms, confirming the feasibility of the proposed upconversion process to release Pt(II).</div></div>","PeriodicalId":364,"journal":{"name":"Journal of Inorganic Biochemistry","volume":"271 ","pages":"Article 112982"},"PeriodicalIF":3.8,"publicationDate":"2025-06-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144518948","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Targeting DNA mismatches with metal complexes","authors":"Natália Kolozsvári,&nbsp;Martin R. Gill","doi":"10.1016/j.jinorgbio.2025.112977","DOIUrl":"10.1016/j.jinorgbio.2025.112977","url":null,"abstract":"<div><div>DNA mismatches are non Watson-Crick base pairs that arise from errors during replication or are the result of DNA damage. Normally repaired by the mismatch mediated repair (MMR) pathway, in cancers deficient in MMR, such as subsets of colorectal and endometrial cancers, mismatches persist and accumulate, providing a biochemical vulnerability creating a target for small-molecule intervention. This review explores how metal complexes employing rhodium(III), ruthenium(II) or platinum(II) centres can exploit this molecular distinction to preferentially bind mismatch sites in DNA. We discuss the potential of this interaction to act as a foundation for next-generation therapeutics and imaging probes where the unique structural, electronic, and photophysical properties of metal complexes and associated ligand design offer opportunities to differentiate between canonical and mismatched DNA with high selectivity.</div></div>","PeriodicalId":364,"journal":{"name":"Journal of Inorganic Biochemistry","volume":"271 ","pages":"Article 112977"},"PeriodicalIF":3.8,"publicationDate":"2025-06-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144513853","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Alternative zinc binding peptides as potential tags for recombinant protein purification","authors":"Richmond A. Adomako,&nbsp;Michael B. Owusu,&nbsp;Airam Cordova,&nbsp;Laurence A. Angel","doi":"10.1016/j.jinorgbio.2025.112981","DOIUrl":"10.1016/j.jinorgbio.2025.112981","url":null,"abstract":"<div><div>Efficient binding of peptides and proteins to metal-chelating resins is a cornerstone of modern biochemical purification. This study evaluates a novel heptapeptide sequence, acetyl-Aa₁-Aa₂-Gly₃-Pro₄-Aa₅-His₆-Cys₇, where Aa₁ = His₁ or Asp₁, Aa₂ = Cys₂ or Asp₂ and Aa₅ = Tyr₅ or Gly₅ for its capacity to bind zinc-chelating resin consisting of divalent zinc chelated by iminodiacetate coupled to 6 % cross-linked agarose beads. Comparisons were made against the widely utilized 7 × His tag using an internal standard method with ion mobility – mass spectrometry analyses and ultra-violet absorption analyses, which quantified the binding efficiency and selectivity of these peptides under pH 8 conditions and the elution from the zinc resin using pH 3.9 or excess imidazole. Results revealed that the heptapeptides acetyl-His₁-Cys₂-Gly₃-Pro₄-Tyr₅-His₆-Cys₇, exhibited binding performance to the zinc chelating resin with conditions commonly used with immobilized metal affinity chromatography and efficient elution from the zinc resin at pH 3.9 or with excess imidazole, suggesting that this heptapeptide has potential as an alternative to polyhistidine tags in affinity-based purification workflows.</div></div>","PeriodicalId":364,"journal":{"name":"Journal of Inorganic Biochemistry","volume":"271 ","pages":"Article 112981"},"PeriodicalIF":3.8,"publicationDate":"2025-06-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144501212","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"The binding of kojic acid dimer and its Zn(II) and Cu(II) complexes at the beta-amyloid peptide: A DFT-based computational assessment","authors":"Iogann Tolbatov ,&nbsp;Tiziano Marzo ,&nbsp;Massimiliano Peana ,&nbsp;Serenella Medici ,&nbsp;Maria Antonietta Zoroddu ,&nbsp;Diego La Mendola ,&nbsp;Alessandro Marrone","doi":"10.1016/j.jinorgbio.2025.112979","DOIUrl":"10.1016/j.jinorgbio.2025.112979","url":null,"abstract":"<div><div>The increasing number of people afflicted by Alzheimer's disease in the world requires a constant intensification of the efforts to seek for new agents capable of dismantling the molecular mechanisms underlying the onset and development of this neurodegenerative disorder. In this study, the binding of kojic acid dimer (KAD), and its adducts with Zn(II) and Cu(II) to the beta-amyloid peptide (Aβ) have been investigated by means of density functional theory-based computational approaches. We envisioned that the capability of KAD to inhibit the amyloid cascade may be exerted in concomitance and/or supported by the coordination of either Zn(II) or Cu(II). Thus, the structure and binding features of KAD-Zn and KAD-Cu metal complexes were computationally assessed to gain an atomistic insight of the possible Aβ inhibition. Our calculations evidenced that Zn(II), but not Cu(II), might act in concert with KAD in the binding of the Aβ peptide. Furthermore, we identified the Aβ₁₃_–₂₀ region as a plausible binding site for KAD and KAD-Zn complexes, emphasizing its relevance for future experimental studies.</div></div>","PeriodicalId":364,"journal":{"name":"Journal of Inorganic Biochemistry","volume":"271 ","pages":"Article 112979"},"PeriodicalIF":3.8,"publicationDate":"2025-06-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144471792","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Exploring the anticancer properties of indenyl and allyl palladates through their interaction with nucleic acids","authors":"Tommaso Giani ,&nbsp;Giannantonio Tomasi ,&nbsp;Pablo A. Nogara ,&nbsp;Laura Orian ,&nbsp;Fabiano Visentin ,&nbsp;Thomas Scattolin ,&nbsp;Tarita Biver","doi":"10.1016/j.jinorgbio.2025.112978","DOIUrl":"10.1016/j.jinorgbio.2025.112978","url":null,"abstract":"<div><div>In this work, we analyse the mechanistic features of the interaction of indenyl (<strong>1-Ind</strong>) and allyl (<strong>2-All</strong>) palladates with nucleic acids (NAs) such as DNA (natural, poly(dA)-poly(dT) and poly(dG)-poly(dC)), RNA (in double and triple helices) and non-canonical structures of DNA (G-quadruplex and i-motif). Spectrophotometric titrations under different temperature and salt content conditions, viscosimetric experiments, fluorescent intercalator displacement (FID) tests together with theoretical Density Functional Theory (DFT)/Docking calculations are used to enlighten the complicated features of the interaction. The binding occurs in the grooves of the polynucleotides and is dominated by the geometrical features of the NA. A strong affinity for RNA double helix is present, together with interesting binding signatures to G-quadruplex and i-motif. The indenyl moiety plays a role and the binding is tighter (<strong>1-Ind</strong> &gt; <strong>2-All</strong>) for all NA systems. However, it is <strong>2-All</strong> that, interestingly, shows the more striking differences in changing from one NA to another. The formation of covalent adducts and other mechanistic features are also discussed.</div></div>","PeriodicalId":364,"journal":{"name":"Journal of Inorganic Biochemistry","volume":"271 ","pages":"Article 112978"},"PeriodicalIF":3.8,"publicationDate":"2025-06-18","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144471791","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Multiple catalytic functions of an engineered double mutant of myoglobin with a potential metal-binding site","authors":"Ai-Qun Pan ,&nbsp;Xi-Chun Liu ,&nbsp;Lu Yu ,&nbsp;Shuai Tang ,&nbsp;Shu-Qin Gao ,&nbsp;Ying-Wu Lin","doi":"10.1016/j.jinorgbio.2025.112976","DOIUrl":"10.1016/j.jinorgbio.2025.112976","url":null,"abstract":"<div><div>Rational protein engineering has emerged as a powerful tool for creating functional enzymes, and the design of metalloenzymes with dual active sites is particularly attractive. In this study, we performed a double mutation of F46H/L49D in the helices C and D region in myoglobin (Mb). As demonstrated by X-ray crystallography, the double mutations preserved the overall Mb fold and formed a potential metal-binding site, located ∼15 Å from the heme iron, which enable the protein to bind various metal ions such as Cu²⁺, Mg²⁺ and others. Moreover, the binding of Cu²⁺/Mg²⁺ conferred multiple enzymatic activities to F46H/L49D Mb. The Cu²⁺-F46H/L49D Mb complex exhibited significant nitrite reductase and superoxide dismutase activities. Notably, the protein exhibited DNA cleavage activity in the presence of Mg²⁺, achieving nearly 100 % cleavage efficiency within 30 min. By demonstrating the versatility of the engineered metal-binding site in Mb, this study suggests that rational design can expand the functional repertoire of the protein. The F46H/L49D Mb mutant serves as a versatile platform for studying metal-dependent catalysis of artificial metalloenzymes with non-heme/heme dual active sites, offering potential applications in biocatalysis, medicine, and industrial catalysis.</div></div>","PeriodicalId":364,"journal":{"name":"Journal of Inorganic Biochemistry","volume":"271 ","pages":"Article 112976"},"PeriodicalIF":3.8,"publicationDate":"2025-06-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144297952","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Cobalt complexes as modulators against amyloid-β aggregation","authors":"Jeasang Yoo ,&nbsp;Jong-Min Suh ,&nbsp;Gunhee Kim ,&nbsp;Hélène Bernard ,&nbsp;Raphaël Tripier ,&nbsp;Dongwook Kim ,&nbsp;Mingeun Kim ,&nbsp;Mi Hee Lim","doi":"10.1016/j.jinorgbio.2025.112972","DOIUrl":"10.1016/j.jinorgbio.2025.112972","url":null,"abstract":"<div><div>The progressive aggregation of amyloid-β (Aβ) peptides is central to the development of Alzheimer's disease, contributing to memory loss, cognitive decline, and neuronal degeneration. Transition metal complexes, owing to their tunable oxidation states and diverse coordination geometries, have been explored as chemical modulators to disrupt the aggregation pathways of Aβ peptides. Their biological applications, however, are often constrained by inherent toxicity and potential metal release. Herein, we report the selection and preparation of cobalt complexes with macrocyclic 1,4,8,11-tetraazacyclotetradecane (<strong>Cyclam</strong>) and 1,8-dimethyl-1,4,8,11-tetraazacyclotetradecane (<strong>DMC</strong>) ligands, [Co(<strong>Cyclam</strong>)(NO₃)](NO₃), [Co(<strong>Cyclam</strong>)(Cl)₂]Cl, [Co(<strong>DMC</strong>)(H₂O)₂](NO₃)₂, and [Co(<strong>DMC</strong>)(Cl)₂]Cl, adopting either <em>trans</em>-III or <em>cis</em>-V geometry as relatively stable chemical reagents for controlling the assembly and toxicity profiles of Aβ peptides. Our mechanistic investigations reveal that these cobalt complexes can form adducts with Aβ peptides and, subsequently, redirect their aggregation pathway away from the canonical on-pathway process towards the formation of amorphous clusters and shorter fibrils. Furthermore, cobalt complexes mitigate Aβ-induced toxicity with minimal intrinsic toxicity in living cells. Overall, our study illustrates a guidance for selecting metal complexes as chemical modulators against Aβ amyloidogenesis by integrating the characteristics of both metal centers and ligand scaffolds.</div></div>","PeriodicalId":364,"journal":{"name":"Journal of Inorganic Biochemistry","volume":"271 ","pages":"Article 112972"},"PeriodicalIF":3.8,"publicationDate":"2025-06-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144297951","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"DNA cleavage and antitumoral activity of zinc(II) and iron(III) complexes with a new phenol-based ligand containing uncoordinated thioether moieties","authors":"Daniele C. Durigon ,&nbsp;Rafaella B. Marinho ,&nbsp;Laura G. Magnabosco ,&nbsp;Tetsade C.B. Piermartiri ,&nbsp;Lucas Göbel ,&nbsp;Carla I. Tasca ,&nbsp;Fernando R. Xavier ,&nbsp;Cláudia B. Nedel ,&nbsp;Adailton J. Bortoluzzi ,&nbsp;Hernán Terenzi ,&nbsp;Rosely A. Peralta","doi":"10.1016/j.jinorgbio.2025.112974","DOIUrl":"10.1016/j.jinorgbio.2025.112974","url":null,"abstract":"<div><div>In this study, a novel ligand: 2-((bis(2-(phenylthio)ethyl)amino)methyl)-6-((bis(pyridin-2-ylmethyl)amino)methyl)-4-methylphenol (<strong>HL</strong>) was prepared and subsequently used to synthesize the complexes [Zn(L)(OAc)]ClO₄ (<strong>1</strong>) and [Fe₂(L)(μ-OAc)(μ-O)](ClO₄)₂ (<strong>2</strong>). The metal complexes were comprehensively characterized using different techniques such as IR, Mass Spectrometry, UV–Vis, elemental analysis and X-ray analysis. The crystal structures show that compound <strong>1</strong> is a mononuclear pentacoordinate zinc(II) complex, while compound <strong>2</strong> is a dinuclear hexacoordinate iron(III) compound, with the metal centers connected by μ-oxo and μ-acetato bridges. In both cases, the phenol-based ligand features thioether substituents as pendant arms. We have evaluated the binding of the new complexes to DNA and also their capacity to cleave it. Both complexes have excellent antitumor activity against an astrocytic tumor derived from a primary human GBM1 cell line.</div></div><div><h3>Synopsis</h3><div>The paper reports synthesis and characterization of two new complexes [Zn(L)(OAc)]ClO₄ (<strong>1</strong>) and [Fe₂(L)(μ-OAc)(μ-O)](ClO₄)₂ (<strong>2</strong>). Complex <strong>1</strong> exhibits better activity than <strong>2</strong> at lower concentrations and with a faster rate of action, showing a preference for the minor groove. The cytotoxicity studies demonstrated a reduction in cell viability when exposed to the complexes, with GBM and C6 cells.</div></div>","PeriodicalId":364,"journal":{"name":"Journal of Inorganic Biochemistry","volume":"271 ","pages":"Article 112974"},"PeriodicalIF":3.8,"publicationDate":"2025-06-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144291491","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}