Oscar Barrios , Claudia Inclán , Pablo Herrera , Alicia Bort , Avelino Martín , Jesús Cano , Inés Díaz-Laviada , Rafael Gómez
{"title":"Ruthenium(II) complexes containing PEGylated N-heterocyclic carbene ligands for tunning biocompatibility in the fight against cancer","authors":"Oscar Barrios , Claudia Inclán , Pablo Herrera , Alicia Bort , Avelino Martín , Jesús Cano , Inés Díaz-Laviada , Rafael Gómez","doi":"10.1016/j.jinorgbio.2024.112765","DOIUrl":"10.1016/j.jinorgbio.2024.112765","url":null,"abstract":"<div><div>A synthetic procedure was designed for the preparation and characterization of Ag and Ru complexes containing NHC ligands functionalized with PEG fragments. Stability studies were conducted to gain insight of the species in water and other solvents like DMSO, or with reagents like imidazole as representative group for histidine amino acid. The presence of Cl atoms instead of H in the 4,5 positions of the N-heterocyclic carbene afforded higher water stability. The complexes containing PEG units must be considered inactive as anticancer agents. To enhance the anticancer activity of PEG-containing complexes, the balance between hydrophilicity and hydrophobicity was adjusted using a silane moiety, and an anionic carbosilane dendrimer as a lipophilic carrier.</div></div>","PeriodicalId":364,"journal":{"name":"Journal of Inorganic Biochemistry","volume":"262 ","pages":"Article 112765"},"PeriodicalIF":3.8,"publicationDate":"2024-10-26","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142542651","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":"A dye-decolorizing peroxidase from Vibrio cholerae can demetallate heme","authors":"Takeshi Uchida , Sayaka Umetsu , Miho Sasaki , Haruka Yoshimura , Issei Omura , Koichiro Ishimori","doi":"10.1016/j.jinorgbio.2024.112764","DOIUrl":"10.1016/j.jinorgbio.2024.112764","url":null,"abstract":"<div><div>Iron is an essential element for bacterial survival. Bacterial pathogens have therefore developed methods to obtain iron. <em>Vibrio cholerae</em>, the intestinal pathogen that causes cholera, utilizes heme as an iron source. DyP from <em>V. cholerae</em> (<em>Vc</em>DyP) is a dye-decolorizing peroxidase. When <em>Vc</em>DyP was expressed in <em>Escherichia coli</em> and purified, it was found to contain protoporphyrin IX (PPIX) but not heme, indicating that the protein possesses deferrochelatase activity. Here, we examined the demetallation reaction of <em>Vc</em>DyP using fluorescence spectroscopy. Treatment of heme-reconstituted <em>Vc</em>DyP with sodium dithionite under anaerobic conditions led to an increase in the fluorescence intensity at 624 nm, suggesting the formation of PPIX. Although the same reaction was conducted using myoglobin, horseradish peroxidase and hemin, no increase in the fluorescence was observed. Therefore, demetallation of heme is specific to <em>Vc</em>DyP. This reaction was faster at lower pH, but the amplitudes of the fluorescence increase were larger at pH 6.5–7.5, in clear contrast to the dye-decolorizing activity with the optimal pH of 4.5. In contrast to HutZ from <em>V. cholerae</em>, which is a heme-degrading enzyme that cleaves the heme macrocycle to release iron, <em>Vc</em>DyP can remove iron from heme without degradation. To our knowledge, <em>Vc</em>DyP is the first enzyme whose demetallation activity has been confirmed at neutral pH. Our results show that <em>Vc</em>DyP is a bifunctional protein that degrades anthraquinone dyes and demetallates heme.</div></div>","PeriodicalId":364,"journal":{"name":"Journal of Inorganic Biochemistry","volume":"262 ","pages":"Article 112764"},"PeriodicalIF":3.8,"publicationDate":"2024-10-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142542649","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}
Callie Miller , Kylie Knutson , Dali Liu , Brian Bennett , Richard C. Holz
{"title":"Catalytic and post-translational maturation roles of a conserved active site serine residue in nitrile hydratases","authors":"Callie Miller , Kylie Knutson , Dali Liu , Brian Bennett , Richard C. Holz","doi":"10.1016/j.jinorgbio.2024.112763","DOIUrl":"10.1016/j.jinorgbio.2024.112763","url":null,"abstract":"<div><div>A highly conserved second-sphere active site αSer residue in nitrile hydratase (NHase), that forms a hydrogen bond with the axial metal-bound water molecule, was mutated to Ala, Asp, and Thr, in the Co-type NHase from <em>Pseudonocardia thermophila</em> JCM 3095 (<em>Pt</em>NHase) and to Ala and Thr in the Fe-type NHase from <em>Rhodococcus equi</em> TG328–2 (<em>Re</em>NHase). All five mutants were successfully purified; metal analysis via ICP-AES indicated that all three Co-type <em>Pt</em>NHase mutants were in their apo-form while the Fe-type αSer117Ala and αSer117Thr mutants contained 85 and 50 % of their active site Fe(III) ions, respectively. The <em>k</em><sub><em>cat</em></sub> values obtained for the <em>Pt</em>NHase mutant enzymes were between 0.03 ± 0.01 and 0.2 ± 0.02 s<sup>−<strong>1</strong></sup> amounting to <0.8 % of the <em>k</em><sub><em>cat</em></sub> value observed for WT <em>Pt</em>NHase. The Fe-type <em>Re</em>NHase mutants retained some detectable activity with <em>k</em><sub><em>cat</em></sub> values of 93 ± 3 and 40 ± 2 s<sup>−<strong>1</strong></sup> for the αSer117Ala and αSer117Thr mutants, respectively, which is ∼5 % of WT <em>Re</em>NHase activity towards acrylonitrile. UV–Vis spectra coupled with EPR data obtained on the <em>Re</em>NHase mutant enzymes showed subtle changes in the electronic environment around the active site Fe(III) ions, consistent with altering the hydrogen bonding interaction with the axial water ligand. X-ray crystal structures of the three <em>Pt</em>NHase mutant enzymes confirmed the mutation and the lack of active site metal, while also providing insight into the active site hydrogen bonding network. Taken together, these data confirm that the conserved active site αSer residue plays an important catalytic role but is not essential for catalysis. They also confirm the necessity of the conserved second-sphere αSer residue for the metalation process and subsequent post-translational modification of the α-subunit in Co-type NHases but not Fe-type NHases, suggesting different mechanisms for the two types of NHases.</div></div><div><h3>Synopsis</h3><div>A strictly conserved active site αSer residue in both Co- and Fe-type nitrile hydratases was mutated. This αSer residue was found to play an important catalytic function, but is not essential. In Co-type NHases, it appears to be essential for active site maturation, but not in Fe-type NHases.</div></div>","PeriodicalId":364,"journal":{"name":"Journal of Inorganic Biochemistry","volume":"262 ","pages":"Article 112763"},"PeriodicalIF":3.8,"publicationDate":"2024-10-18","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142492277","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}
Md Shofiul Alam , Jonathan Cedeño , Michael A. Reyes , Sebastian Scavuzzo , Jaroslava Miksovska
{"title":"Interactions of Li+ ions with NCS1: A potential mechanism of Li+ neuroprotective action against psychotic disorders","authors":"Md Shofiul Alam , Jonathan Cedeño , Michael A. Reyes , Sebastian Scavuzzo , Jaroslava Miksovska","doi":"10.1016/j.jinorgbio.2024.112762","DOIUrl":"10.1016/j.jinorgbio.2024.112762","url":null,"abstract":"<div><div>Li<sup>+</sup> based drugs have been used for the treatment of psychiatric disorders due to their mood stabilizing role for decades. Recently, several studies reported the protective effect of Li<sup>+</sup> against severe neuropathologies such as Parkinson's, Alzheimer's, and Huntington's disease. Surprisingly, despite a broad range of Li<sup>+</sup> effects on neurological conditions, little is known about its molecular mechanism. In this study, we propose that neuronal calcium sensor 1 (NCS1), can be an effective molecular target for Li<sup>+</sup> action. Here we show that the EF-hands in ApoNCS1 have submillimolar affinity for Li<sup>+</sup> with K<sub>d</sub> = 223 ± 19 μM. Li<sup>+</sup> binding to ApoNCS1 quenches Trp emission intensity, suggesting distinct Trp sidechains environment in Li<sup>+</sup>NCS1 compared to ApoNCS1 and Ca<sup>2+</sup>NCS1. Li<sup>+</sup> association also stabilizes the protein α-helical structure, in a similar way to Ca<sup>2+</sup>. Li<sup>+</sup> association does not promote NCS1 dimerization. Association of Li<sup>+</sup> increases NCS1 affinity for the D2R receptor binding peptide, in a similar way to Ca<sup>2+</sup>, however, the affinity of NCS1 for chlorpromazine is reduced with respect to Ca<sup>2+</sup>NCS1, possibly due to a decrease in solvent exposed hydrophobic area on the NCS1 surface in the presence of Li<sup>+</sup>. MD simulation data suggests that Li<sup>+</sup> ions are coordinated by four oxygens from Asp and Glu sidechains and one carbonyl oxygen, in a similar way as reported previously for Li<sup>+</sup> binding to DREAM. Overall, the data shows that Li<sup>+</sup> binds to EF-hands of NCS1 and Li<sup>+</sup>NCS1 interactions may be involved in the potential neuroprotective role of Li<sup>+</sup> against psychotic disorders.</div></div>","PeriodicalId":364,"journal":{"name":"Journal of Inorganic Biochemistry","volume":"262 ","pages":"Article 112762"},"PeriodicalIF":3.8,"publicationDate":"2024-10-18","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142492278","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":"Positively charged residues play a significant role in enhancing the antibacterial activity of calcitermin","authors":"Silvia Leveraro , Maria D'Accolti , Erika Marzola , Elisabetta Caselli , Remo Guerrini , Magdalena Rowinska-Zyrek , Maurizio Remelli , Denise Bellotti","doi":"10.1016/j.jinorgbio.2024.112761","DOIUrl":"10.1016/j.jinorgbio.2024.112761","url":null,"abstract":"<div><div>A systematic study on the human antimicrobial peptide calcitermin (VAIALKAAHYHTHKE) and its carefully designed derivatives was undertaken to verify the impact of divalent copper and zinc ions on the stability, coordination and antimicrobial activity of the formed complexes. In this work we investigate the calcitermin mutants where the alanine in position 7 and 8 is substituted with an arginine residue, with the aim of enhancing the antibacterial activity. Additionally, the analogue where alanine in position 7 is replaced with a histidine is considered, to obtain a chelating sequence with four histidines in alternate position; the aim of this change was to increase the cationic properties of the peptide under acidic conditions and possibly enhance its binding ability towards the metal ions. Through a comprehensive analytical approach involving potentiometric titrations, mass spectrometry, UV–Vis spectrophotometry, NMR and circular dichroism, we delved into the formation equilibria and coordination chemistry of the formed copper(II) and zinc(II) complexes. Antimicrobial assays are also performed to assess the bioactivity of the compounds against a broad spectrum of microorganisms, revealing the pivotal role of positively charged residues in enhancing the antibacterial activity of calcitermin. The obtained results serve as an important stepping stone towards the development of novel metal-based antimicrobial agents.</div></div>","PeriodicalId":364,"journal":{"name":"Journal of Inorganic Biochemistry","volume":"262 ","pages":"Article 112761"},"PeriodicalIF":3.8,"publicationDate":"2024-10-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142454990","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}
Jinhua Xie , Shahedul Islam , Le Wang , Xiaojing Zheng , Mengsheng Xu , Xiqi Su , Shaohua Huang , Logan Suits , Guang Yang , Prahathees Eswara , Jianfeng Cai , Li-June Ming
{"title":"A tale of two old drugs tetracycline and salicylic acid with new perspectives—Coordination chemistry of their Co(II) and Ni(II) complexes, redox activity of Cu(II) complex, and molecular interactions","authors":"Jinhua Xie , Shahedul Islam , Le Wang , Xiaojing Zheng , Mengsheng Xu , Xiqi Su , Shaohua Huang , Logan Suits , Guang Yang , Prahathees Eswara , Jianfeng Cai , Li-June Ming","doi":"10.1016/j.jinorgbio.2024.112757","DOIUrl":"10.1016/j.jinorgbio.2024.112757","url":null,"abstract":"<div><div>Extensive use of the broad-spectrum tetracycline antibiotics (TCs) has resulted their wide spread in the environment and drive new microecological balances, including the infamous antibiotic resistance. TCs require metal ions for their antibiotic activity and resistance via interactions with ribosome and tetracycline repressor TetR, respectively, at specific metal-binding sites. Moreover, the Lewis-acidic metal center(s) in metallo-TCs can interact with Lewis-basic moieties of many bioactive secondary metabolites, which in turn may alter their associated chemical equilibria and biological activities. Thus, it is ultimately important to reveal detailed coordination chemistry of metallo-TC complexes. Herein, we report (a) conclusive specific Co<sup>2+</sup>, Ni<sup>2+</sup>, and Cu<sup>2+</sup>-binding of TC revealed by paramagnetic <sup>1</sup>H NMR, showing different conformations of the coordination and different metal-binding sites in solution and solid state, (b) significant metal-mediated activity of Cu-TC toward catechol oxidation with different mechanisms by air and H<sub>2</sub>O<sub>2</sub> (i.e., mono- and di-nuclear pathways, respectively), (c) interactions of metallo-TCs with bioactive salicylic acid and its precursor benzoic acid, and (d) noticeable change of TC antibiotic activity by metal and salicylic acid. The results imply that TCs may play broad and versatile roles in maintaining certain equilibria in microecological environments in addition to their well-established antibiotic activity. We hope the results may foster further exploration of previously unknown metal-mediated activities of metallo-TC complexes and other metalloantibiotics.</div></div>","PeriodicalId":364,"journal":{"name":"Journal of Inorganic Biochemistry","volume":"262 ","pages":"Article 112757"},"PeriodicalIF":3.8,"publicationDate":"2024-10-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142445869","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}
Tao Shao , Zhihui Feng , Yu Shen , Dandan Chen , Pan Xiang , Qiong Zhang , Shao Ma , Yupeng Tian , Xiaohe Tian
{"title":"Fine-tuning the side-chain length of iridium(III) complexes for enhanced Photophysical properties in Cancer Theranostics","authors":"Tao Shao , Zhihui Feng , Yu Shen , Dandan Chen , Pan Xiang , Qiong Zhang , Shao Ma , Yupeng Tian , Xiaohe Tian","doi":"10.1016/j.jinorgbio.2024.112760","DOIUrl":"10.1016/j.jinorgbio.2024.112760","url":null,"abstract":"<div><div>Cyclometalated iridium(III) complexes have emerged as versatile candidates for cancer theranostics, offering integrated diagnostic imaging and potent singlet oxygen (<sup>1</sup>O<sub>2</sub>) generation for photodynamic therapy (PDT). However, their application has been limited by subdued photoluminescence, primarily due to intramolecular motion-induced excited energy dissipation. In this study, we address these limitations through the design and synthesis of five novel iridium(III) complexes: <strong>IrC2</strong>, <strong>IrC4</strong>, <strong>IrC6</strong>, <strong>IrC8</strong>, and <strong>IrC12</strong>. Our approach employs meticulous side-chain extending strategy to modulate side-chain length, thereby reducing intramolecular motion and significantly enhancing both one- and three-photon emissions and <sup>1</sup>O<sub>2</sub> production in the aggregated state. Detailed photophysical investigations, supported by crystallographic insights, reveal that side-chain elongation substantially amplifies these properties. Among the synthesized complexes, <strong>IrC8</strong> stands out as a superior candidate for image-guided photodynamic therapy in cellular and 3D tumor spheroid models. This investigation pioneers the simultaneous enhancement of dual-photon emissions and PDT efficacy through a novel side-chain extension strategy in iridium(III) complexes, paving the way for their translational application in clinical theranostics.</div></div>","PeriodicalId":364,"journal":{"name":"Journal of Inorganic Biochemistry","volume":"262 ","pages":"Article 112760"},"PeriodicalIF":3.8,"publicationDate":"2024-10-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142442299","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":"Copper(II) complexes containing hydrazone and bipyridine/phenanthroline ligands for anticancer application against breast cancer cells","authors":"Dorothy Priyanka Dorairaj , Prashant Kumar , Haritha Rajasekaran , Nattamai Bhuvanesh , Sodio C.N. Hsu , Ramasamy Karvembu","doi":"10.1016/j.jinorgbio.2024.112759","DOIUrl":"10.1016/j.jinorgbio.2024.112759","url":null,"abstract":"<div><div>In this work, mixed ligand Cu(II) complexes containing hydrazone and bipyridine ligands (<strong>CB1</strong>-<strong>CB5</strong>), or hydrazone and phenanthroline ligands (<strong>CP1</strong>-<strong>CP5</strong>) have been synthesized and characterized by spectroscopic and analytical techniques. Single crystal X-ray structure of complex <strong>CB1</strong> revealed that two nitrogen atoms from bipyridine, one carbonyl oxygen, one azomethine nitrogen and one hydroxyl oxygen from the hydrazone ligand coordinated to Cu(II) ion, adopting a distorted square pyramidal geometry. Interaction of these complexes with calf thymus (CT) DNA and bovine serum albumin (BSA) was analyzed by absorption and emission studies. Further, the <em>in vitro</em> anticancer activity of the complexes was investigated exclusively against the breast cancer cells namely MCF7, T47D and MDA MB 231, and a normal breast MCF 10a cell line. The phenanthroline bearing complexes (<strong>CP1</strong>-<strong>CP5</strong>) displayed better activity than their bipyridine counterparts as seen from the IC<sub>50</sub> values. In addition, the most active complex <strong>CP1</strong> having an IC<sub>50</sub> value of 5.8 ± 0.3 μM against T47D cancer cells was investigated for its mode of cell death through acridine orange/ethidium bromide(AO/EB), 4′,6-diamidino-2-phenylindole (DAPI) and Annexin-V fluorescein isothiocyanate (FITC) staining assays which revealed apoptosis. Lastly, the cell cycle analysis revealed that complex <strong>CP1</strong> induced cell death in T47D cancer cells at the G0/G1 phase.</div></div>","PeriodicalId":364,"journal":{"name":"Journal of Inorganic Biochemistry","volume":"262 ","pages":"Article 112759"},"PeriodicalIF":3.8,"publicationDate":"2024-10-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142454988","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":"Two bis-maltol-polyamines: Synthesis, characterization and studies of their palladium(II) complexes exploring their potential anticancer activity","authors":"Daniele Paderni , Eleonora Macedi , Enrica Sordini , Stefano Amatori , Patrizia Rossi , Mauro Formica , Luca Giorgi , Paola Paoli , Mirco Fanelli , Vieri Fusi","doi":"10.1016/j.jinorgbio.2024.112758","DOIUrl":"10.1016/j.jinorgbio.2024.112758","url":null,"abstract":"<div><div>The interest in the antineoplastic and binding properties shown by the bis-maltol polyamine family, particularly Malten and Maltonis, prompted us to study the Pd<sup>2+</sup> complexes of these latter from both a biological and metallo-receptor point of view. The Malten-Pd<sup>2+</sup> complex can lodge hard species such as Sr<sup>2+</sup> in its coordination-driven preorganized pocket, as confirmed by X-ray diffraction. UV–Vis and NMR data showed that Malten-Pd<sup>2+</sup> forms even at acidic pH and exists in aqueous solution in a wide range of pH. The mononuclear complex is stable enough not to release Pd<sup>2+</sup> in solution for a long period of time (at least one week), thus Malten-Pd<sup>2+</sup>, similarly to Maltonis-Pd<sup>2+</sup>, is suitable to be tested in biological analyses. Studies on the U937 cell line revealed that the effect on cell survival reduction induced by Malten is partially lost in Malten-Pd<sup>2+</sup>, while no differences where monitored between the effects of Maltonis-Pd<sup>2+</sup> and Maltonis, suggesting that the availability of free maltol moieties, that is retained in Maltonis-Pd<sup>2+</sup>, but not in Malten-Pd<sup>2+</sup>, is crucial to guarantee the biological activity of these compounds.</div></div>","PeriodicalId":364,"journal":{"name":"Journal of Inorganic Biochemistry","volume":"262 ","pages":"Article 112758"},"PeriodicalIF":3.8,"publicationDate":"2024-10-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142405842","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":"AIE-based ruthenium complexes as photosensitizers for specifically photo-inactivate gram-positive bacteria","authors":"Hai-Yan Huang , Run-Yu Xue , Su-Xin Xiao , Li-Ting Huang , Xiang-Wen Liao , Jin-Tao Wang , Xue-Min Duan , Ru-Jian Yu , Yan-Shi Xiong","doi":"10.1016/j.jinorgbio.2024.112755","DOIUrl":"10.1016/j.jinorgbio.2024.112755","url":null,"abstract":"<div><div>The emergence of multidrug-resistant bacterial have caused severe burden for public health. Particularly, <em>Staphylococcus aureus</em> as one of ESKAPE pathogens have induced various infectious diseases and resulted in increasing deaths. Developing new antibacterial agents is still urgent and challenging. Fortunately, in this study, based on aggregation-induced emission (AIE) ruthenium complexes were designed and synthesized, which realized the high efficiency of reactive oxygen species generation and remarkably killed <em>S. aureus</em> unlike conventional antibiotics action. Significantly, owing to good singlet oxygen production ability, <strong>Ru1</strong> at only 4 μg/mL of concentration displayed good antibacterial photodynamic therapy effect upon white light irradiation and could deplete essential coenzyme NADH to disrupt intracellular redox balance. Also, the electrostatic interaction between <strong>Ru1</strong> and bacteria enhanced the possibility of antibacterial. Under light irradiation, <strong>Ru1</strong> could efficiently inhibit the biofilm growth and avoid the development of drug-resistant. Furthermore, <strong>Ru1</strong> possessed excellent biocompatibility and displayed remarkable therapy effect in treating mice-wound infections in vivo. These findings indicated that AIE-based ruthenium complexes as new antibacterial agent had great potential in photodynamic therapy of bacteria and addressing the drug-resistance crisis.</div></div>","PeriodicalId":364,"journal":{"name":"Journal of Inorganic Biochemistry","volume":"262 ","pages":"Article 112755"},"PeriodicalIF":3.8,"publicationDate":"2024-10-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142398990","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}