Journal of Inorganic Biochemistry最新文献

{"title":"Repaglinide platinum(IV) conjugates: Enhancing p53 signaling for antitumor and antimetastatic efficacy","authors":"Suying Li ,&nbsp;Zhifang Liu ,&nbsp;Yan Chen ,&nbsp;Shuaiqi Feng ,&nbsp;Hengye Chen ,&nbsp;Yanna Zhao ,&nbsp;Yanqin He ,&nbsp;Qingpeng Wang","doi":"10.1016/j.jinorgbio.2025.112910","DOIUrl":"10.1016/j.jinorgbio.2025.112910","url":null,"abstract":"<div><div>The tumor suppressor p53 plays multiple roles at the crossroads of suppressing tumor development and metastasis. Here, a series of Repaglinide platinum(IV) conjugates promoting the p53 pathway were designed and prepared, which displayed potent antiproliferative and antimetastatic activities both <em>in vitro</em> and <em>in vivo</em>. Mechanistically, the expression of p53 was upregulated by the synergistic functions of the platinum core through causing severe DNA damage, and the RPG ligand <em>via</em> stimulating the lumican/p53/p21 pathway. The mitochondria-mediated apoptosis was initiated, involving the Bcl-2/Bax/caspase pathway. Pro-death autophagy was initiated with the upregulation of LC3II and down regulation of p62. Additionally, angiogenesis was suppressed by reversing tumor inflammation through the inhibition of key enzymes COX-2, MMP9, and VEGFA. Furthermore, antitumor immunity was enhanced by blocking the immune checkpoint PD-L1, which led to an increased presence of CD3⁺ and CD8⁺ T-cells within the tumor microenvironment.</div></div>","PeriodicalId":364,"journal":{"name":"Journal of Inorganic Biochemistry","volume":"268 ","pages":"Article 112910"},"PeriodicalIF":3.8,"publicationDate":"2025-04-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143791269","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":"Unraveling the unfolding mechanism of pseudoazurin: Insights into stabilizing cupredoxin fold as a common domain of Cu-containing proteins","authors":"Takahide Yamaguchi ,&nbsp;Attila Taborosi ,&nbsp;Kiyokazu Tsugane ,&nbsp;Kathleen Wood ,&nbsp;Andrew E. Whitten ,&nbsp;Seiji Mori ,&nbsp;Takamitsu Kohzuma","doi":"10.1016/j.jinorgbio.2025.112907","DOIUrl":"10.1016/j.jinorgbio.2025.112907","url":null,"abstract":"<div><div>Understanding protein unfolding mechanisms is crucial for comprehending protein-folding related diseases, developing diagnostic methods, and designing proteins with desired stability for medicinal or industrial applications. However, investigating structures at atomic resolution is often difficult due to the flexibility and transiency of unfolding intermediate states. Pseudoazurin (PAz) is a well-characterized simple cupredoxin composed of a small polypeptide (124 amino acids) and a single metal cofactor (Cu²⁺), making it suitable to study the unfolding mechanism. In this study, combining the merits of structure determination by small-angle neutron scattering (SANS) and molecular dynamics (MD) simulations enabled us to access the details of the unfolding mechanism. The unfolding of PAz proceeds through a two-step mechanism involving the “native”, “open-domain”, and “random-coil” states. Several amino acid residues at the vicinity of Cu²⁺ ion are involved in the structural transitions, where the interactions among these residues are important in controlling the stability of PAz. These findings may be applicable to stabilizing metalloproteins with cupredoxin domain structures.</div></div>","PeriodicalId":364,"journal":{"name":"Journal of Inorganic Biochemistry","volume":"268 ","pages":"Article 112907"},"PeriodicalIF":3.8,"publicationDate":"2025-04-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143791271","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Rationalizing the structural basis of organic-platinum hybrid complexes binding towards quadruplex-duplex hybrids through all-atom simulations","authors":"Salvatore Muscarella,&nbsp;Irene Treccarichi,&nbsp;Luisa D'Anna,&nbsp;Angelo Spinello","doi":"10.1016/j.jinorgbio.2025.112904","DOIUrl":"10.1016/j.jinorgbio.2025.112904","url":null,"abstract":"<div><div>Guanine-rich sequences containing complementary base pairs can fold into non-canonical quadruplex-duplex hybrid (QDH) conformations. These structures possess unique structural features, leading to the presence of a peculiar binding pocket that can be distinguished from a canonical double helix or a G-quadruplex (G4) structure. Recently, two organic-metal hybrid platinum complexes, able to selectively and strongly recognize a particular type of QDH with a lateral duplex stem-loop, were reported in the literature. However, solution structures are not available for all the investigated compounds, leaving unanswered questions on the structural traits underlying the different binding affinity of these complexes. In this work, we address this gap using all-atom simulations to unravel the key features driving the high selectivity of these organic‑platinum hybrid complexes at an atomistic level. In particular, their binding affinity depends on a delicate balance between the extended π-π stacking interactions performed in the G4-duplex binding pocket and the capacity to form stable hydrogen bonds with the surrounding nucleobases. Thus, our findings provide essential insights to guide the rational design of novel compounds that selectively target QDH structures.</div></div>","PeriodicalId":364,"journal":{"name":"Journal of Inorganic Biochemistry","volume":"268 ","pages":"Article 112904"},"PeriodicalIF":3.8,"publicationDate":"2025-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143785778","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Bioinspired copper(II) complexes catalyzed oxidative coupling of aminophenols with broader substrate scope","authors":"Thasnim P Mohammed ,&nbsp;Marappan Velusamy ,&nbsp;Muniyandi Sankaralingam","doi":"10.1016/j.jinorgbio.2025.112906","DOIUrl":"10.1016/j.jinorgbio.2025.112906","url":null,"abstract":"<div><div>The strategic selection of ligand systems in metal complexes has demonstrated a profound impact on the efficiency and specificity of biomimetic reactions. In this work, we introduce a series of aminoquinoline-based copper(II) complexes (<strong>1</strong>–<strong>4</strong>) distinguished by systematic variation in terminal amine substituents: di-<em>n</em>-methyl (<strong>L1</strong>(H)), di-<em>n</em>-ethyl (<strong>L2</strong>(H)), di-<em>n</em>-propyl (<strong>L3</strong>(H)), and di-<em>n</em>-butyl (<strong>L4</strong>(H)). These complexes are synthesized, characterized, and evaluated as the catalyst for the oxidative coupling of different aminophenol derivatives. Remarkably, complex <strong>1</strong>, featuring a methyl substituent, exhibited unparalleled catalytic performance, achieving an 86 % (<em>K</em>_cat - 9.7 × 10⁴ h⁻¹) conversion of <em>o</em>-aminophenol to the desired product, 2-amino-phenoxazin-3-one, alongside water and hydrogen peroxide as byproducts. Notably, complex <strong>1</strong> demonstrated exceptional versatility, extending its catalytic activity to other substrates with remarkable activity. Mechanistic investigations, supported by mass-spectrometric analysis, revealed the formation of a complex-substrate adduct with all substrates, enabling us to propose a detailed reaction pathway. The work highlights the benefits of ligand design in improving catalytic performance and sets a new standard for aminoquinoline-based copper(II) complexes in oxidative coupling reactions. To the best of our knowledge, this work is the first to report a wider substrate scope for PHS activity with copper(II) complexes.</div></div>","PeriodicalId":364,"journal":{"name":"Journal of Inorganic Biochemistry","volume":"270 ","pages":"Article 112906"},"PeriodicalIF":3.8,"publicationDate":"2025-03-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143829668","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":"Ascorbic acid potentiates the formation of IgG-enriched protein aggregates in plasma in a Cu(II)-mediated manner","authors":"Christian Saporito-Magriña ,&nbsp;Lila Lopez-Montañana ,&nbsp;María Laura Facio ,&nbsp;Guadalupe Pagano ,&nbsp;Topp Nicole ,&nbsp;Ariana Danzi ,&nbsp;Juan Ignacio Bellida ,&nbsp;Agustín Silva ,&nbsp;Matías Albizzati ,&nbsp;Marisa Gabriela Repetto","doi":"10.1016/j.jinorgbio.2025.112905","DOIUrl":"10.1016/j.jinorgbio.2025.112905","url":null,"abstract":"<div><div>Protein aggregates have been reported in disease but also in physiological contexts in tissues as well as circulating protein aggregates in the bloodstream. Free Cu(II) induces the aggregation of serum proteins and this metal yields highly oxidant species upon reaction with hydrogen peroxide and also reacts with ascorbic acid (AA). A broad population is exposed to high doses of AA as second line therapy for different pathologies or as nutritional supplementation. This study addresses the effect of AA on the formation of plasma protein aggregates, observed by optic density, protein quantification and electrophoresis (SDS-PAGE) that, contrary to hampering the Cu(II)-induced plasma protein aggregation, AA potentiates their formation. Free Cu(II) induces the formation of IgG-enriched plasma protein aggregates but the combination with AA potentiates the incorporation of gamma-globulin (IgG) whereas other proteins such as albumin become depleted. The potentiating effect of Cu(II) and AA was corroborated employing isolated IgG. This effect of AA on Cu(II)-induced protein aggregation is not reproduced with isolated albumin. Additionally, AA does not potentiate Fe(III)-mediated aggregation of IgG, albumin or human plasma. Finally, it was shown that in healthy subjects which were administered high doses of intravenous AA, the aggregates can be obtained from the centrifuged plasma after 30 min of the administration of the antioxidant. Aggregated IgG have been shown to activate Fc receptors, involved in oxidative burst and inflammatory processes observed in neutrophils. Thus, the effect of AA on the immune system could be linked to the accumulation of protein aggregates enriched in specific proteins.</div></div>","PeriodicalId":364,"journal":{"name":"Journal of Inorganic Biochemistry","volume":"269 ","pages":"Article 112905"},"PeriodicalIF":3.8,"publicationDate":"2025-03-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143705198","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":"Coiled coils as ligands for inclusion in the inorganic chemist's toolbox – For advances in MRI contrast agent design","authors":"Anna F.A. Peacock","doi":"10.1016/j.jinorgbio.2025.112903","DOIUrl":"10.1016/j.jinorgbio.2025.112903","url":null,"abstract":"<div><div>Ligands are essential tools in synthetic inorganic chemistry, enabling the fine-tuning of metal ion properties to optimize performance. Spanning from small molecules to macromolecular proteins, ligands vary widely in structure and function. De novo designed coiled coils serve as a unique bridge between these extremes, offering precise control over metal coordination. Here, we explore the application of coiled coil ligands in MRI contrast agent design, leveraging their versatility to systematically modulate the coordination chemistry and hydration state of gadolinium - the metal used in most clinical MRI contrast agents. This novel class of gadolinium-based agents demonstrates superior performance compared to existing clinical agents, highlighting the potential of coiled coil ligands. Furthermore, when coordinated to copper, these ligands form complexes that challenge the conventional notion that copper is unsuitable for MRI contrast agents. These findings establish coiled coil ligands as a powerful platform for advancing contrast agent design.</div></div>","PeriodicalId":364,"journal":{"name":"Journal of Inorganic Biochemistry","volume":"268 ","pages":"Article 112903"},"PeriodicalIF":3.8,"publicationDate":"2025-03-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143762780","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":"Novel erbium complex with anticancer activity against radiation resistant lung adenocarcinoma cells","authors":"Hao Wang ,&nbsp;Guozhu Ren ,&nbsp;Yue Xu ,&nbsp;Ruiping Deng ,&nbsp;Rui Wang ,&nbsp;Liang Zhou","doi":"10.1016/j.jinorgbio.2025.112902","DOIUrl":"10.1016/j.jinorgbio.2025.112902","url":null,"abstract":"<div><div>In this work, novel erbium complex with anticancer activity against radiation resistant lung adenocarcinoma cells was obtained and demonstrated. Firstly, stronger inhibitory effect of Er³⁺ on non-small cell lung cancer (NSCLC) cells and NSCLC- radiation resistant (RR) cells was experimentally confirmed. Then, by selecting highly biocompatible porphyrins as ligands, a novel erbium complex tetraphenylporphyrin erbium acetylacetonate (Er(acac)TPP) was synthesized and purified. Compared with Cisplatin, notably, Er(acac)TPP exhibits relatively higher inhibitory efficiency on NSCLC-RR cells. Moreover, the toxicities of Er(acac)TPP to normal cells are much lower than that of cancer cells. Subsequently, cell expansion, increased apoptosis, a decline in mitochondrial membrane potential (MMP), an accumulation of intracellular reactive oxygen species (ROS), increased Caspase-9 protein level and G2/M arrest were seen. These data all pointed to Er(acac)TPP as a possible candidate for more research and development as a chemotherapeutic drug.</div></div>","PeriodicalId":364,"journal":{"name":"Journal of Inorganic Biochemistry","volume":"269 ","pages":"Article 112902"},"PeriodicalIF":3.8,"publicationDate":"2025-03-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143682899","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":"An insight into porphyrin carbamate derivatives and a Cu(II) metalloporphyrin as G-quadruplex binder: Synthesis, single crystal characterization, binding ability and anti-tumor potential","authors":"Xinyan Zou ,&nbsp;Wenting Xiao ,&nbsp;Xiang Zhou ,&nbsp;Rui Shen ,&nbsp;Aihong Yang ,&nbsp;Xiaodi Kou","doi":"10.1016/j.jinorgbio.2025.112901","DOIUrl":"10.1016/j.jinorgbio.2025.112901","url":null,"abstract":"<div><div>Telomere with a G-quadruplex (Gq) structure is a recognized anti-tumor target. It was found that the aromatic plane of porphyrin may form π-π interactions with the Gq structure and the coordination of metal ions to porphyrin may increase its aromatic plane. Therefore, in this work, two porphyrin carbamate derivatives (<strong>1</strong> and <strong>2</strong>) and a Cu(II) metalloporphyrin (<strong>1-Cu</strong>) were designed and synthesized. The single crystals of <strong>1</strong> and <strong>1-Cu</strong> were obtained and characteristics related to the binding interactions were analyzed at molecular level. With further Hirshfeld surface, molecular electrostatic potential, and frontier molecular orbital analyses, it was revealed that porphyrin ring, phenyl carbamate side chain and the coordinated copper ion may form synergistic binding forces with the Gq structure. Subsequently, binding ability and binding mode were tested with UV–Vis, fluorescence, and circular dichroism spectroscopies and PCR-stop method. Result showed that all three compounds selectively bound to Gq with the highest binding constant of 3.19 × 10⁷, which was an order of magnitude higher than those to the duplex DNA. Further molecular docking and molecular dynamics simulations supported the synergistic end stacking and groove binding modes. At last, anti-tumor potentials were evaluated with cytotoxicity, cell staining, cell apoptosis, and cell migration assays. Results showed that compared with the positive control drug, the IC₅₀ values of <strong>1</strong> and <strong>1-Cu</strong> to the tumor cells were significantly lower, and their cytotoxicities to tumor cells were much higher than those to normal cells. Therefore, this work provided important information for designing novel drugs targeting Gq telomere.</div></div>","PeriodicalId":364,"journal":{"name":"Journal of Inorganic Biochemistry","volume":"269 ","pages":"Article 112901"},"PeriodicalIF":3.8,"publicationDate":"2025-03-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143673124","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":"An oral delivery approach for riboflavin-targeted platinum(II)-loaded lipid nanoparticles into alginate-gelatin matrices against 2D and 3D colorectal carcinoma models","authors":"Tugce Boztepe ,&nbsp;Federico Karp ,&nbsp;Silvia Cabrera ,&nbsp;José Aleman ,&nbsp;Diego G. Lamas ,&nbsp;Cristián Huck-Iriart ,&nbsp;Germán A. Islan ,&nbsp;Ignacio E. León","doi":"10.1016/j.jinorgbio.2025.112900","DOIUrl":"10.1016/j.jinorgbio.2025.112900","url":null,"abstract":"<div><div>This study investigated the use of riboflavin-targeted Nanostructured Lipid Carriers (R-NLCs) to deliver a platinum-based anticancer drug [PtCl(8-O-quinolinate)(dmso)] (8-QO-Pt) to colorectal cancer cells. Three different R-8-QO-Pt-NLC formulations were prepared via hot-homogenization by ultrasonication method. The physicochemical characterizations of NLCs were analyzed by small- and wide-angle X-ray scattering (SAXS/WAXS) and fourier transformed infrared spectroscopy (FTIR). The cytotoxic effects and IC₅₀ values of R-8-QO-Pt-NLC formulations were compared with those of the free 8-QO-Pt. Cellular uptake and apoptosis were evaluated towards HCT 116 cells in monolayer (2D). The liquid overlay technique was used to generate 3D multicellular tumor spheroids, MCTS. The anticancer and antimetastatic activities of the free 8-QO-Pt and R-8-QO-Pt-NLCs were determined in MCTS. The results revealed that R-8-QO-Pt-NLC exhibited greater cytotoxicity and lower IC₅₀ values than free 8-QO-Pt in both 2D and 3D cell cultures. Furthermore, results showed that the volumes of the spheroids were reduced in response to increasing concentrations of R-8-QO-Pt-NLC, showing higher inhibition of cell migration in colorectal cancer spheroids at concentrations of 10.0, 15.0, and 25.0 μM than free 8-QO-Pt. To provide protection against gastric acid conditions, an additional drug delivery system based on alginate (Alg) and gelatin (Gel) beads for R-8-QO-Pt-NLC oral administration was developed. While free and R-NLC encapsulated 8-QO-Pt were practically inactivated at pH 1.2 and 37 °C, it was revealed that the Alg-Gel beads retain 5.7 times the initial activity of the R-8-QO-Pt-NLC. The findings of this research indicate that R-8-QO-Pt-NLC embedded in Alg-Gel beads are promising hydrogels for targeted colorectal delivery systems.</div></div>","PeriodicalId":364,"journal":{"name":"Journal of Inorganic Biochemistry","volume":"269 ","pages":"Article 112900"},"PeriodicalIF":3.8,"publicationDate":"2025-03-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143734922","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":"Broadening the chemical diversity of oxidovanadium(V) complexes for targeting neglected tropical diseases","authors":"Gonzalo Scalese ,&nbsp;Nicolás Pérez ,&nbsp;Josefina Pereyra ,&nbsp;Yasmina Sanabria ,&nbsp;Olivier Blacque ,&nbsp;Ignacio Machado ,&nbsp;Leticia Pérez-Díaz ,&nbsp;Dinorah Gambino","doi":"10.1016/j.jinorgbio.2025.112891","DOIUrl":"10.1016/j.jinorgbio.2025.112891","url":null,"abstract":"<div><div>Chagas disease and Leishmaniasis, caused by <em>Trypanosoma cruzi</em> and <em>Leishmania spp.</em>, respectively, are highly prevalent neglected tropical diseases (NTDs) that pose significant global health challenges. In our pursuit of effective vanadium-based therapeutics against these diseases, we previously developed several series of oxidovanadium(V) complexes featuring bidentate bioactive ligands and Schiff base tridentate ligands. The current study extends our previous research by incorporating in the same molecule, a tridentate bromo-substituted isonicotinyl hydrazone Schiff base ligand, BrIS, and a 8-hydroxyquinoline derivative (L), leading to the synthesis and comprehensive characterization of five new complexes, [V^VO(BrIS-2H)(L-H)]. Most of new complexes exhibited activity in the micromolar range against the infective trypomastigote form of <em>T. cruzi</em> (EC_{50, 24h}: 0.73–7.95 μM) and against <em>L. infantum</em> promastigotes (IC_{50, 5 days}: 1.14–1.16 μM) and some of them showed good selectivity indexes towards the parasites (SI up to 52). Notably, the vanadium uptake by the parasites was higher for the new [V^VO(BrIS-2H)(L-H)] compounds compared to [V^VO(IN-2H)(L-H)] analogues previously developed, where IN is the structurally related 2-hydroxy-1-naphtaldehyde isonicotinoylhydrazone ligand, with accumulation in the soluble cell fraction. High-dose incubations resulted in trypanocidal effects and suggested the generation of reactive oxygen species (ROS). Further analysis revealed that [V^VO(BrIS-2H)(L-H)] complexes induced a higher percentage of apoptosis, whereas the [V^VO(IN-2H)(L-H)] series was associated with autophagic cell death. These findings highlight the potential of the [V^VO(BrIS-2H)(L-H)] series as promising anti-<em>T. cruzi</em> agents and underscore the need for further research to optimize their therapeutic efficacy and explore their mechanisms of action.</div></div>","PeriodicalId":364,"journal":{"name":"Journal of Inorganic Biochemistry","volume":"269 ","pages":"Article 112891"},"PeriodicalIF":3.8,"publicationDate":"2025-03-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143668695","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}