Journal of Inorganic Biochemistry最新文献

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Jim Kincaid and heme proteins: The Princeton years and beyond
IF 3.8 2区 化学
Journal of Inorganic Biochemistry Pub Date : 2025-01-25 DOI: 10.1016/j.jinorgbio.2025.112834
Thomas G. Spiro
{"title":"Jim Kincaid and heme proteins: The Princeton years and beyond","authors":"Thomas G. Spiro","doi":"10.1016/j.jinorgbio.2025.112834","DOIUrl":"10.1016/j.jinorgbio.2025.112834","url":null,"abstract":"<div><div>This article is a personal chronical of Jim Kincaid's scientific career from his postdoctoral years in my laboratory at Princeton, to his final years in his lab at Marquette. He devoted himself to the study of heme proteins, using Raman spectroscopy as a probe of structure and function, producing many notable advances in our understanding of these key biological molecules. Along the way, Jim supported and encouraged many aspiring scientists. Reminiscences from his students and colleagues affirm his enthusiasm for science and for friendship, his generosity of time and attention, his puckish sense of humor, his unfailing kindness and his concern for the well-being of those around him, to the very end of his life. I was fortunate to have him as a student, collaborator, and life-long friend.</div></div>","PeriodicalId":364,"journal":{"name":"Journal of Inorganic Biochemistry","volume":"266 ","pages":"Article 112834"},"PeriodicalIF":3.8,"publicationDate":"2025-01-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143073367","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}
引用次数: 0
Two multifunctional zero-dimensional Gd(III) complexes: magnetocaloric effect and anticancer mechanisms for lung cancer
IF 3.8 2区 化学
Journal of Inorganic Biochemistry Pub Date : 2025-01-22 DOI: 10.1016/j.jinorgbio.2025.112832
Shouying Cao, Yaqing Xie, Xiaotong Lu, Zijie Zhao, Feiya Zhou, Jie Wang, Lili Liang
{"title":"Two multifunctional zero-dimensional Gd(III) complexes: magnetocaloric effect and anticancer mechanisms for lung cancer","authors":"Shouying Cao,&nbsp;Yaqing Xie,&nbsp;Xiaotong Lu,&nbsp;Zijie Zhao,&nbsp;Feiya Zhou,&nbsp;Jie Wang,&nbsp;Lili Liang","doi":"10.1016/j.jinorgbio.2025.112832","DOIUrl":"10.1016/j.jinorgbio.2025.112832","url":null,"abstract":"<div><div>Two Gd(III) complexes [GdL(H<sub>2</sub>O)(NO<sub>3</sub>)<sub>2</sub>(CH<sub>3</sub>OH)<sub>0.75</sub>(CH<sub>3</sub>CH<sub>2</sub>OH)<sub>0.25</sub>] (<strong>Gd1</strong>) and [Gd<sub>2</sub>(OOCCH<sub>3</sub>)<sub>2</sub>L<sub>2</sub>(H<sub>2</sub>O)<sub>6</sub>]•2(H<sub>2</sub>O) (<strong>Gd2</strong>) (HL = 2-pyridylcarboxaldehyde isonicotinoylhydrazone) were synthesized with a Schiff base ligand. Crystallographic study reveals both <strong>Gd1</strong> and <strong>Gd2</strong> have a zero-dimensional mononuclear or binuclear structure. Magnetic investigations demonstrate that <strong>Gd1</strong> and <strong>Gd2</strong> exhibit potential magnetocaloric effects due to Gd(III) ions, which provide negligible magnetic anisotropy, and possess low-lying excited spin states. The antiproliferative activity of <strong>Gd1</strong> and <strong>Gd2</strong> to three tumor cell lines was conducted and the results showed <strong>Gd1</strong> and <strong>Gd2</strong> showed more pronounced antiproliferative activity to A549 cells better than cisplatin. The administration of <strong>Gd1</strong> and <strong>Gd2</strong> led to an increase in apoptosis among A549 cells in a concentration-dependent manner, along with a corresponding rise in the levels of reactive oxygen species (ROS) within the cells. Besides, <strong>Gd1</strong> and <strong>Gd2</strong> were able to significantly inhibit tumor cell migration. Cell cycle assay in A549 cells revealed that cell cycle was arrested of G0/G1 phase. Western blotting analysis showed that <strong>Gd1</strong> and <strong>Gd2</strong> complexes could promote apoptosis in A549 cells by modulating the expression of Bcl-2 and Bax proteins.</div></div>","PeriodicalId":364,"journal":{"name":"Journal of Inorganic Biochemistry","volume":"265 ","pages":"Article 112832"},"PeriodicalIF":3.8,"publicationDate":"2025-01-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143057437","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}
引用次数: 0
Copper-nitrite complexes release nitric oxide and selectively induce oral precancer and cancer cell apoptosis
IF 3.8 2区 化学
Journal of Inorganic Biochemistry Pub Date : 2025-01-20 DOI: 10.1016/j.jinorgbio.2025.112833
Yen-Yun Wang , Pang-Yu Chen , Naorem Jemes Meitei , Yu-Ren Lin , Tsai-Te Lu , Hieu D.H. Nguyen , Sodio C.N. Hsu , Shyng-Shiou F. Yuan
{"title":"Copper-nitrite complexes release nitric oxide and selectively induce oral precancer and cancer cell apoptosis","authors":"Yen-Yun Wang ,&nbsp;Pang-Yu Chen ,&nbsp;Naorem Jemes Meitei ,&nbsp;Yu-Ren Lin ,&nbsp;Tsai-Te Lu ,&nbsp;Hieu D.H. Nguyen ,&nbsp;Sodio C.N. Hsu ,&nbsp;Shyng-Shiou F. Yuan","doi":"10.1016/j.jinorgbio.2025.112833","DOIUrl":"10.1016/j.jinorgbio.2025.112833","url":null,"abstract":"<div><div>Nitric oxide (NO) is a small, short-lived gas molecule that influences various critical functions in living organisms<strong>.</strong> It involves multiple physiological processes, including cardiovascular function, metabolism, neurotransmission, immunity, and aberrant NO signaling leads to various disorders such as cardiovascular diseases, diabetes, and cancers. In this study, we explored the potential application of copper-nitrite complexes in treating oral precancer and cancer. The copper-nitrite complexes, L<sub>1</sub>Cu(NO<sub>2</sub>) and L<sub>2</sub>Cu(NO<sub>2</sub>), were shown to release NO into cells and selectively induce cytotoxicity to oral precancer and cancer cells. Notably, L<sub>1</sub>Cu(NO<sub>2</sub>) inhibited oral cancer cell proliferation by causing G0/G1 phase cell cycle arrest. Furthermore, L<sub>1</sub>Cu(NO<sub>2</sub>) induced cell apoptosis and upregulated the expression of p-PRAS40 (proline-rich Akt substrate of 40 kDa) in oral cancer cells. All these results reveal the therapeutic potential of copper-nitrite complexes, especially L<sub>1</sub>Cu(NO<sub>2</sub>), to be developed as a targeted therapy against oral precancer and cancer.</div></div>","PeriodicalId":364,"journal":{"name":"Journal of Inorganic Biochemistry","volume":"265 ","pages":"Article 112833"},"PeriodicalIF":3.8,"publicationDate":"2025-01-20","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143035694","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}
引用次数: 0
Large-capacity DNA vectors based on rolling circle amplification with multivalent aptamers delivery copper sulfide for the synergistic treatment of Cancer through chemo/Photothermal/Chemodynamic therapy in vitro
IF 3.8 2区 化学
Journal of Inorganic Biochemistry Pub Date : 2025-01-17 DOI: 10.1016/j.jinorgbio.2025.112831
Huan Du, Fang Wang, Ruyan Zhang, Yan Ma, Xiaobing Huo, Gan Ning, Xiufeng Wang, Ting Zhou, Guodong Zhang, Zhiqing Zhang
{"title":"Large-capacity DNA vectors based on rolling circle amplification with multivalent aptamers delivery copper sulfide for the synergistic treatment of Cancer through chemo/Photothermal/Chemodynamic therapy in vitro","authors":"Huan Du,&nbsp;Fang Wang,&nbsp;Ruyan Zhang,&nbsp;Yan Ma,&nbsp;Xiaobing Huo,&nbsp;Gan Ning,&nbsp;Xiufeng Wang,&nbsp;Ting Zhou,&nbsp;Guodong Zhang,&nbsp;Zhiqing Zhang","doi":"10.1016/j.jinorgbio.2025.112831","DOIUrl":"10.1016/j.jinorgbio.2025.112831","url":null,"abstract":"<div><div>Developing multifunctional nanomedicines represents a frontier. We have engineered a high-capacity DNA vector basing rolling circle amplification for the delivery of copper sulfide nanoparticles (CuS NPs) and doxorubicin (DOX), coupled with multivalent aptamers (MA) that precisely target tumors, culminating in a multifunctional nanoplatform (RMAL<sub>1</sub>Cu@DOX), which combines the chemotherapy (CT)/photothermal therapy (PTT)/chemodynamic therapy (CDT). The vector (RMAL<sub>1</sub>) boasts exceptional biocompatibility and incorporates multiple copy units, enabling the precise loading of numerous CuS NPs, forming RMAL<sub>1</sub>Cu which possesses a robust photothermal effect and superior Fenton-like catalytic activity, heralding a project of minimally invasive dual-mode (PTT/CDT) therapy. Furthermore, the abundance of G-C of RMAL<sub>1</sub> enabled effective DOX encapsulation through π-π interactions to construct RMAL<sub>1</sub>Cu@DOX. The MA integrated into RMAL<sub>1</sub>Cu@DOX is pivotal in enhancing the targeting of tumors and in preventing non-specific release of CuS and DOX, enabling an integrated CT/PTT/CDT. Data indicate that 1 nM of RMAL<sub>1</sub>Cu could load 270 nM of DOX with an impressive loading capacity of 77 %, and modification with MA, its tumor-targeting ability was amplified by 51-fold and significantly bolstered in vitro imaging outcomes, and the synergistic killing of B16 was as 67.3 %. This innovative nanoplatform offers a comprehensive and holistic strategy for the treatment of malignant tumors.</div></div>","PeriodicalId":364,"journal":{"name":"Journal of Inorganic Biochemistry","volume":"265 ","pages":"Article 112831"},"PeriodicalIF":3.8,"publicationDate":"2025-01-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143035696","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}
引用次数: 0
Binding a C12-appended rhenium-(Bispyridine) carbonyl complex to β-Lactoglobulin: Effects of pH & cysteine modification on calyx affinity 将 C12 添加的铼-(双吡啶)羰基复合物与 β-乳球蛋白结合:pH 值和半胱氨酸修饰对花萼亲和力的影响。
IF 3.8 2区 化学
Journal of Inorganic Biochemistry Pub Date : 2025-01-13 DOI: 10.1016/j.jinorgbio.2025.112828
Emily E. Stumbo , Sean T. Goralski , Phillip R. Leclair, Spencer Kerns, Michael J. Rose
{"title":"Binding a C12-appended rhenium-(Bispyridine) carbonyl complex to β-Lactoglobulin: Effects of pH & cysteine modification on calyx affinity","authors":"Emily E. Stumbo ,&nbsp;Sean T. Goralski ,&nbsp;Phillip R. Leclair,&nbsp;Spencer Kerns,&nbsp;Michael J. Rose","doi":"10.1016/j.jinorgbio.2025.112828","DOIUrl":"10.1016/j.jinorgbio.2025.112828","url":null,"abstract":"<div><div>Due to its commercial availability and well-defined structure, the interaction between bovine protein β-lactoglobulin (βLG) and a wide variety of non-native ligands — including transition metal complexes — has been explored, but its application as an artificial metalloenzyme scaffold is limited. This protein is hypothesized to transport fatty acids and other nutrients during juvenile development, and it binds hydrophobic ligands inside a binding pocket constructed upon an 8-stranded β-barrel, called the ‘calyx’. Herein, we compare the binding behavior of two rhenium(anthracene-bispyridine) (‘Anth-py<sub>2</sub>’) tricarbonyl complexes, one with a 12‑carbon chain appended to the ligand scaffold (‘<sup>C12</sup>Anth-py<sub>2</sub>’) to βLG. We investigate (<em>i</em>) how calyx-binding specificity is affected by pH (which controls βLG structure at the entrance to the calyx) and (<em>ii</em>) modification of a free cysteine residue located in a putative second binding site of βLG (SMe-βLG). The binding affinities of [Re(<sup>C12</sup>Anth-py<sub>2</sub>)(CO)<sub>3</sub>(solv)]<sup>+</sup> (ReC<sub>12</sub>) and [Re(Anth-py<sub>2</sub>)(CO)<sub>3</sub>(solv)]<sup>+</sup> (ReCH) for βLG at pH 7.3 were similar at 36 ± 2 μM and 43 ± 1 μM, respectively. The K<sub>D</sub> of ReC<sub>12</sub> decreased by ∼13 μM at pH 6.1 due to a well-known conformational change (Tanford transition) at the entrance to the calyx; the K<sub>D</sub> value was not significantly affected by Cys121 modification, indicating β-barrel calyx binding specificity. In contrast, ReCH experienced a decrease in K<sub>D</sub> in response to blocking the second binding (SMe-βLG), but was also unaffected by pH. The results show an increase in binding affinity and specificity as a result of targeted ligand design and utilization of native protein characteristics. The findings will inform and improve the design of future βLG-derived ArMs.</div></div>","PeriodicalId":364,"journal":{"name":"Journal of Inorganic Biochemistry","volume":"265 ","pages":"Article 112828"},"PeriodicalIF":3.8,"publicationDate":"2025-01-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143035690","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}
引用次数: 0
Nitrite binding to myoglobin and hemoglobin: Reactivity and structural aspects
IF 3.8 2区 化学
Journal of Inorganic Biochemistry Pub Date : 2025-01-11 DOI: 10.1016/j.jinorgbio.2025.112829
Paolo Ascenzi , Giovanna De Simone , Gabriele Antonio Zingale , Massimo Coletta
{"title":"Nitrite binding to myoglobin and hemoglobin: Reactivity and structural aspects","authors":"Paolo Ascenzi ,&nbsp;Giovanna De Simone ,&nbsp;Gabriele Antonio Zingale ,&nbsp;Massimo Coletta","doi":"10.1016/j.jinorgbio.2025.112829","DOIUrl":"10.1016/j.jinorgbio.2025.112829","url":null,"abstract":"<div><div>Nitrite (NO<sub>2</sub><sup>−</sup>) interacts with myoglobin (Mb) and hemoglobin (Hb) behaving as a ligand of both the ferrous (<em>i.e.</em>, Mb(II) and Hb(II)) and ferric (<em>i.e.</em>, Mb(III) and Hb(III)) forms. However, while the binding to the Fe(III) species corresponds to the formation of a stable complex (<em>i.e.</em>, Mb(III)-NO<sub>2</sub><sup>−</sup> and Hb(III)-NO<sub>2</sub><sup>−</sup>), in the case of the ferrous forms the reaction proceeds with a nitrite reductase redox process, leading to the oxidation of the heme-protein with the reduction of NO<sub>2</sub><sup>−</sup> to NO. This event is of the utmost importance for the rapid production of NO <em>in vivo</em> in the blood stream and in striated muscles, being crucial for the regulation of the blood flow, and thus for O<sub>2</sub> supply to poorly oxygenated tissues, such as the eye's retina. Further, NO<sub>2</sub><sup>−</sup> interacts with Mb(II)-O<sub>2</sub> and Hb(II)-O<sub>2</sub>, inducing their oxidation with a complex mechanism, which has been only partially elucidated. Mb and Hb form the complex with NO<sub>2</sub><sup>−</sup> through the <em>O</em>-nitrito binding mode (<em>i.e.</em>, Fe-ONO<sup>−</sup>), which is regulated by residues paving the heme distal side; thus, in a site-directed mutant, where HisE7 is substituted by Val, the interaction occurs in the <em>N</em>-nitro binding mode (<em>i.e.</em>, Fe-N(<em>O</em>)O<sup>−</sup>), like in most other heme-proteins. The structure-function relationships of the interaction of NO<sub>2</sub><sup>−</sup> with both ferric and ferrous forms of Mb and Hb are discussed here.</div></div>","PeriodicalId":364,"journal":{"name":"Journal of Inorganic Biochemistry","volume":"265 ","pages":"Article 112829"},"PeriodicalIF":3.8,"publicationDate":"2025-01-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143035710","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}
引用次数: 0
Palladium(II) complexes containing andrographolide appended N,O heterocyclic chelators: Investigation of anti-oxidant, anti-cancer and apoptotic activities
IF 3.8 2区 化学
Journal of Inorganic Biochemistry Pub Date : 2025-01-11 DOI: 10.1016/j.jinorgbio.2025.112830
Priya Prasad , S. Parveen , Abdullah A. Alarfaj , Abdurahman Hajinur Hirad , M. Mohamed Subarkhan , S. Dhanapal , G. Kalaiarasi
{"title":"Palladium(II) complexes containing andrographolide appended N,O heterocyclic chelators: Investigation of anti-oxidant, anti-cancer and apoptotic activities","authors":"Priya Prasad ,&nbsp;S. Parveen ,&nbsp;Abdullah A. Alarfaj ,&nbsp;Abdurahman Hajinur Hirad ,&nbsp;M. Mohamed Subarkhan ,&nbsp;S. Dhanapal ,&nbsp;G. Kalaiarasi","doi":"10.1016/j.jinorgbio.2025.112830","DOIUrl":"10.1016/j.jinorgbio.2025.112830","url":null,"abstract":"<div><div>A series of new Pd(II) complexes were synthesized from the reaction of andrographolide appended hydrazide derivatives with potassium tetrachloropalladate K<sub>2</sub>[PdCl<sub>4</sub>]. The formation of the complexes was confirmed through structural assessments conducted using various spectroscopic techniques. From the spectral studies we confirmed that the ligands coordinated to Pd(II) ion <em>via</em> amine nitrogen and enone oxygen. The complexes were assessed for their antioxidant properties, demonstrating significant radical scavenging activity with a series of free radicals such as 1,1-diphenyl-2-picrylhydrazyl (DPPH<sup>•</sup>), 2,2′-azinobis-(3-ethylbenzothiazoline-6-sulphonic acid diammonium salt (ABTS<sup>•+</sup>), Super oxide (O<sup>2−</sup>) and Nitric oxide (NO<sup>•</sup>) radicals compared with standard antioxidants. Moreover, <em>in vitro</em> antiproliferative investigations conducted on A549 (human lung cancer) and HeLa (human cervical cancer) cell lines revealed significant cytotoxicity of the complexes, with lower IC<sub>50</sub> values compared to the standard metallo-drug <em>cisplatin</em>. Morphological alterations observed in HeLa and A549 cells when treated with IC<sub>50</sub> concentrations of the complexes, as examined through Acridine Orange-Ethidium Bromide (AO-EB) and 4′,6-diamidino-2-phenylindole (DAPI) staining techniques, indicated cell death <em>via</em> apoptosis. Biological studies indicated that AGC-Pd exhibited superior activity among others, further the percentages of the apoptotic and necrotic cells were determined by flow cytometric technique.</div></div>","PeriodicalId":364,"journal":{"name":"Journal of Inorganic Biochemistry","volume":"265 ","pages":"Article 112830"},"PeriodicalIF":3.8,"publicationDate":"2025-01-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143027661","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}
引用次数: 0
Accessing iridium Cp* as a cofactor for artificial metalloenzymes 获得铱Cp*作为人工金属酶的辅助因子。
IF 3.8 2区 化学
Journal of Inorganic Biochemistry Pub Date : 2025-01-03 DOI: 10.1016/j.jinorgbio.2024.112820
Oskar James Klein, Armando Albert-Flores, Matthew G. Wheeler, Katherine Rojales, Andrew D. Bond, Sally R. Boss, Paul D. Barker
{"title":"Accessing iridium Cp* as a cofactor for artificial metalloenzymes","authors":"Oskar James Klein,&nbsp;Armando Albert-Flores,&nbsp;Matthew G. Wheeler,&nbsp;Katherine Rojales,&nbsp;Andrew D. Bond,&nbsp;Sally R. Boss,&nbsp;Paul D. Barker","doi":"10.1016/j.jinorgbio.2024.112820","DOIUrl":"10.1016/j.jinorgbio.2024.112820","url":null,"abstract":"<div><div>By introducing new-to-nature transformations, artificial metalloenzymes hold great potential for expanding the biosynthetic toolbox. The chemistry of an active cofactor in these enzymes is highly dependent on how the holoprotein is assembled, potentially limiting the choice of organometallic complexes amenable to incorporation and ability of the protein structure to influence the metal centre. We have previously reported a method utilising ligand exchange as a means to introduce ruthenium-arene fragments into a four-helix bundle protein. In this work we expand the scope of this method to incorporate an iridium pentamethylcyclopentadienyl fragment into a four-helix bundle, yielding an artificial metalloenzyme with improved transfer hydrogenation properties, highlighting that understanding ligand exchange reactions is important for speciation control.</div></div>","PeriodicalId":364,"journal":{"name":"Journal of Inorganic Biochemistry","volume":"265 ","pages":"Article 112820"},"PeriodicalIF":3.8,"publicationDate":"2025-01-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142969166","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}
引用次数: 0
Ruthenium(II)-mercapto complexes induce cell damage via apoptosis pathway on ovarian cancer cells 钌(II)-巯基复合物通过凋亡途径诱导卵巢癌细胞损伤。
IF 3.8 2区 化学
Journal of Inorganic Biochemistry Pub Date : 2024-12-30 DOI: 10.1016/j.jinorgbio.2024.112819
Marcos V. Palmeira-Mello , Tamara Teixeira , Matheus Reis Santos de Melo , Heloiza Diniz Nicolella , Jocely L. Dutra , Marcia R. Cominetti , Fillipe Vieira Rocha , Denise Crispim Tavares , Alzir A. Batista
{"title":"Ruthenium(II)-mercapto complexes induce cell damage via apoptosis pathway on ovarian cancer cells","authors":"Marcos V. Palmeira-Mello ,&nbsp;Tamara Teixeira ,&nbsp;Matheus Reis Santos de Melo ,&nbsp;Heloiza Diniz Nicolella ,&nbsp;Jocely L. Dutra ,&nbsp;Marcia R. Cominetti ,&nbsp;Fillipe Vieira Rocha ,&nbsp;Denise Crispim Tavares ,&nbsp;Alzir A. Batista","doi":"10.1016/j.jinorgbio.2024.112819","DOIUrl":"10.1016/j.jinorgbio.2024.112819","url":null,"abstract":"<div><div>Ovarian cancer represents a leading cause of cancer-related deaths in women worldwide. Chemotherapeutic agents are usually employed to treat the patients, and Ruthenium(II)-based compounds have been investigated as possible substitutes for platinum drugs. In this work, we studied three different Ru(II)-phosphine-mercapto complexes (<strong>1–3</strong>) as potential cytotoxic agents against A2780 and A2780-<em>cis</em>R ovarian cancer cells. A time-dependent cytotoxicity was observed for <strong>2</strong>, which also exhibited better selectivity than cisplatin control. A similar cytotoxic behavior was observed on 3D tumor spheroids. Although no changes were observed in cell cycle distribution, compound <strong>2</strong> affected the mitochondrial membrane potential on A2780 cells, and caused cell death <em>via</em> apoptotic pathway, which was confirmed by flow cytometry assay. Western blotting experiments revealed that <strong>2</strong> affected the expression of p53, PCNA, γH2AX and cleaved caspase-3, making it a promising anticancer agent for ovarian cancer.</div></div>","PeriodicalId":364,"journal":{"name":"Journal of Inorganic Biochemistry","volume":"265 ","pages":"Article 112819"},"PeriodicalIF":3.8,"publicationDate":"2024-12-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142930398","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}
引用次数: 0
Corrigendum to “Spectrofluorimetric analysis of the binding of a target molecule to serum albumin: tricky aspects and tips” [Journal of Inorganic Biochemistry 216 (2021) 111305] “靶分子与血清白蛋白结合的荧光光谱分析:棘手的方面和提示”[无机生物化学杂志216(2021)111305]的勘误表。
IF 3.8 2区 化学
Journal of Inorganic Biochemistry Pub Date : 2024-12-28 DOI: 10.1016/j.jinorgbio.2024.112817
Francesca Macii , Tarita Biver
{"title":"Corrigendum to “Spectrofluorimetric analysis of the binding of a target molecule to serum albumin: tricky aspects and tips” [Journal of Inorganic Biochemistry 216 (2021) 111305]","authors":"Francesca Macii ,&nbsp;Tarita Biver","doi":"10.1016/j.jinorgbio.2024.112817","DOIUrl":"10.1016/j.jinorgbio.2024.112817","url":null,"abstract":"","PeriodicalId":364,"journal":{"name":"Journal of Inorganic Biochemistry","volume":"264 ","pages":"Article 112817"},"PeriodicalIF":3.8,"publicationDate":"2024-12-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142902479","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}
引用次数: 0
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