Journal of Inorganic Biochemistry最新文献

{"title":"A 4-phenylbutyric acid-conjugated platinum diimine complex: Photocytotoxicity, cell cycle arrest and apoptosis in vitro","authors":"Xuemei Guo,&nbsp;Yuxin Lu,&nbsp;Xu Zhang,&nbsp;Xin Wang,&nbsp;Hongfei Wang,&nbsp;Zhigang Zhang","doi":"10.1016/j.jinorgbio.2025.112930","DOIUrl":"10.1016/j.jinorgbio.2025.112930","url":null,"abstract":"<div><div>4-phenylbutyric acid (PBA) is a class <strong>I</strong> and <strong>II</strong> histone deacetylase inhibitor, which can decrease cell proliferation, enhance cell differentiation, and induce apoptosis and cell cycle arrest in various cancer cells. PBA-modified photoactive platinum diimine complex has been prepared and characterized to augment its photodynamic therapy efficacy. Its ability to generate singlet oxygen, behavior in the presence of esterase, photocytotoxicity, cell cycle distribution, and apoptosis-inducing ability in MCF-7 cells have also been studied. The results suggested that the PBA-modified platinum diimine complex could act as a good singlet oxygen producer, release PBA in the presence of esterase, induce potent photocytotoxicity in tumor cells with a IC₅₀ value of 3.67 ± 0.67 μM, arrest cell cycle at S phase, and induce cell death <em>via</em> apoptosis with the percentage of total apoptotic cells being 34.65 %. The results also revealed that PBA might be able to modulate the mode of cell cycle arrest induced by the photosensitizer in tumor cells.</div></div>","PeriodicalId":364,"journal":{"name":"Journal of Inorganic Biochemistry","volume":"270 ","pages":"Article 112930"},"PeriodicalIF":3.8,"publicationDate":"2025-04-18","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143852036","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 interplay between the myeloperoxidase-hypochlorous acid system, heme oxygenase, and free iron in inflammatory diseases","authors":"Mia M. Biernat ,&nbsp;Olivia G. Camp ,&nbsp;Daniel N. Moussa ,&nbsp;Awoniyi O. Awonuga ,&nbsp;Husam M. Abu-Soud","doi":"10.1016/j.jinorgbio.2025.112927","DOIUrl":"10.1016/j.jinorgbio.2025.112927","url":null,"abstract":"<div><div>Accumulated unbound free iron (Fe(II or III)) is a redox engine generating reactive oxygen species (ROS) that promote oxidative stress and inflammation. Iron is implicated in diseases with free radical pathology including cardiovascular, neurodegenerative, reproductive disorders, and some types of cancer. While many studies focus on iron overload disorders, few explore the potential link between the myeloperoxidase-hypochlorous acid (MPO-HOCl) system and localized iron accumulation through heme and iron‑sulfur (Fe<img>S) cluster protein destruction. Although inducible heme oxygenase (HO-1), the rate-limiting enzyme in heme catabolism, is frequently associated with these diseases, we hypothesize that HOCl also contributes to the generation of free iron and heme degradation products. Furthermore, HO-1 and HOCl may play a dual role in free iron accumulation by regulating the activity of key iron metabolism proteins. Enzymatic and non-enzymatic modulators, as well as scavengers of HOCl, can help prevent heme destruction and reduce the accumulation of free iron. Given iron's role in disease progression and severity, identifying the primary sources, mechanisms, and mediators involved in free iron generation is crucial for developing effective pharmacological treatments. Further investigation focusing on the specific contributions of the MPO-HOCl system and free iron is necessary to explore novel strategies to mitigate its harmful effects in biological systems.</div></div>","PeriodicalId":364,"journal":{"name":"Journal of Inorganic Biochemistry","volume":"270 ","pages":"Article 112927"},"PeriodicalIF":3.8,"publicationDate":"2025-04-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143858946","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":"Interaction of half-sandwich Rh(III) ion and some of its complexes with endogenous imidazole derivatives","authors":"Azza A. Hassoon ,&nbsp;Attila Szorcsik ,&nbsp;Tamás Gajda","doi":"10.1016/j.jinorgbio.2025.112913","DOIUrl":"10.1016/j.jinorgbio.2025.112913","url":null,"abstract":"<div><div>An increasing number of {Rh(η⁵-Cp*)}²⁺ complexes are reported to possess promising medical, mostly anticancer activities. In parallel, growing interest has also focused on the interactions between {Rh(η⁵-Cp*)}²⁺-based metallodrugs and macromolecular components of biological fluids, since the biospeciation of these potential metallodrugs may strongly influence their overall pharmacological properties. Less attention was paid to the interaction of {Rh(η⁵-Cp*)}²⁺ complexes with low molecular mass (LMM) constituents of biological fluids, which may also have significant impact on their biospeciation. From this point of view, the biogenic imidazole derivatives are the most important, since the primary binding sites of proteins for {Rh(η⁵-Cp*)}²⁺ cation are the surface histidine groups. Several imidazole containing endogenous LMM components are known, which have relevant concentrations in certain biological fluids, such as plasma. Therefore, here we report systematic solution thermodynamic and solution structural (potentiometric, UV–Vis, ESI-MS and ¹H NMR) study on the interaction of {Rh(η⁵-Cp*)}²⁺ cation with thyrotropin-releasing hormone (TRH, pGlu-His-Pro-NH₂, <strong>L</strong>^{<strong>1</strong>}), carnosine (β-alanyl-histidine, <strong>L</strong>^{<strong>2</strong>}), carcinine (β-alanyl-histamine, <strong>L</strong>^{<strong>3</strong>}), histidine (<strong>L</strong>^{<strong>4</strong>}) and the human growth modulator tripeptide GHK (Gly-His-Lys, <strong>L</strong>^{<strong>5</strong>}). The results indicate, that these biogenic ligands, especially histidine and GHK, possess very high binding ability towards {Rh(η⁵-Cp*)}²⁺ cation, higher than for the well-known histidine-peptide binder copper(II). In addition, we also studied the interaction of two simple [Rh(η⁵-Cp*)(A)Cl]⁺ complexes (where A = 2,2′-bipyridyl (<strong>bpy</strong>) or ethylenediamine (<strong>en</strong>)), as mimics of potentially anticancer compounds, with the above listed endogenous imidazole derivatives. Beside the formation of ternary [Rh(η⁵-Cp*)(A)(L)] complexes, histidine and GHK, having exceptionally high {Rh(η⁵-Cp*)}²⁺ binding ability, are also able to displace <strong>en</strong> or <strong>bpy</strong> from the coordination sphere of Rh(III). Moreover, histidine and GHK successfully compete even with human serum albumin under near physiological conditions, and thus may have fundamental effect on the blood transport and biodistribution of any {Rh(η⁵-Cp*)}²⁺-based bioactive compounds.</div></div>","PeriodicalId":364,"journal":{"name":"Journal of Inorganic Biochemistry","volume":"270 ","pages":"Article 112913"},"PeriodicalIF":3.8,"publicationDate":"2025-04-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143829667","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":"Antiproliferative activity in breast cancer cells of PtL2: A steroid-thiosemicarbazone platinum(II) complex","authors":"Jorge Melones-Herrero ,&nbsp;Francisco Aguilar-Rico ,&nbsp;Ana I. Matesanz ,&nbsp;Carmela Calés ,&nbsp;Isabel Sánchez-Pérez ,&nbsp;Adoracion G. Quiroga","doi":"10.1016/j.jinorgbio.2025.112923","DOIUrl":"10.1016/j.jinorgbio.2025.112923","url":null,"abstract":"<div><div>Breast cancer remains one of the most diagnosed cancers in women worldwide. Metallodrugs such as cisplatin are used in advanced stages and hormone independent tumors. We hereby report the synthesis and characterization of a new benzaldehyde thiosemicarbazone functionalized with an estradiol derivative, LH, and two metal complexes, PdCl₂(LH) and PtL₂. Both complexes were studied in solution showing enough stability to further perform antitumoral activity studies. The Pd(II) complex was discarded for its poor performance while PtL₂ exhibited similar cytotoxic activity to cisplatin (CDDP) in estrogen receptor (+) and triple-negative breast cancer cells. Moreover, PtL₂ demonstrated reduced toxicity in healthy cell lines. It induced cell cycle arrest at the G0/G1 phase, distinguishing its mechanism of action from CDDP, which predominantly blocks cells in the S phase. Additionally, PtL₂ displayed a balanced intracellular distribution between the nucleus and cytoplasm, independent of estrogen receptor status. Further analysis revealed that PtL₂ dysregulated antioxidant enzyme expression, potentially disrupting redox homeostasis. These findings highlight PtL₂’s potential as a promising alternative to conventional platinum-based therapies, warranting further investigation into its molecular mechanisms and therapeutic applications.</div></div>","PeriodicalId":364,"journal":{"name":"Journal of Inorganic Biochemistry","volume":"270 ","pages":"Article 112923"},"PeriodicalIF":3.8,"publicationDate":"2025-04-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143845316","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":"New oxaliplatin-zoledronate derivatives with potential antitumor activity towards bone tumors and metastases","authors":"Alessandra Barbanente ,&nbsp;Anna Maria Di Cosola ,&nbsp;Mauro Niso ,&nbsp;Luisa D'Anna ,&nbsp;Simona Rubino ,&nbsp;Sergio Indelicato ,&nbsp;Concetta Pacifico ,&nbsp;Alessio Terenzi ,&nbsp;Nicola Margiotta","doi":"10.1016/j.jinorgbio.2025.112916","DOIUrl":"10.1016/j.jinorgbio.2025.112916","url":null,"abstract":"<div><div>Bone cancer can originate from any cellular element of the bone and may occur sporadically or as a result of degeneration from a precursor lesion. Bone metastases, often stemming from primary cancers such as breast and prostate cancer, are extremely painful and challenging to treat. The treatment of primary bone malignancies typically involves surgery, radiotherapy, chemotherapy and analgesics. Platinum (Pt)-based drugs are effective against bone cancers and metastases but are often limited by severe side effects due to poor specificity. To improve drug targeting and reduce systemic toxicity, bisphosphonate (BP) ligands, which selectively accumulate in bone tissue, have been combined with Pt-based drugs. The combination of Pt drugs with bisphosphonates like zoledronic acid (ZL) could lead to enhanced therapeutic outcomes due to its intrinsic pharmacological activity. In this study, we report the synthesis and full characterization of two new dinuclear Pt(II) complexes that combine ZL with clinically approved oxaliplatin and the drug-candidate kiteplatin, respectively. These complexes were tested for their stability under physiological and acidic conditions, reactivity with 5’-GMP interaction with B- and G-quadruplex DNA models and cytotoxicity against a panel of human tumor cell lines.</div></div>","PeriodicalId":364,"journal":{"name":"Journal of Inorganic Biochemistry","volume":"270 ","pages":"Article 112916"},"PeriodicalIF":3.8,"publicationDate":"2025-04-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143833377","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":"Structural related oxidovanadium(IV)-flavonoid complexes. Influence on their anticancer effects","authors":"Alexandra Velásquez Bravo ,&nbsp;Juan J. Martínez Medina ,&nbsp;Libertad L. López Tevez ,&nbsp;Andrés G. Restrepo ,&nbsp;Ángel L. Huamaní ,&nbsp;Pablo J. Gonzalez ,&nbsp;Luciana G. Naso ,&nbsp;Evelina G. Ferrer ,&nbsp;Patricia A.M. Williams","doi":"10.1016/j.jinorgbio.2025.112915","DOIUrl":"10.1016/j.jinorgbio.2025.112915","url":null,"abstract":"<div><div>Flavonoids, known for their antioxidant properties in plants, can also act as pro-oxidants in cancer cells, an effect that intensifies when coordinated with metal cations. Among them, oxidovanadium(IV) (VO) complexes with flavonoids have shown promising anticancer potential, following a clear relationship of the ligand structure with the activity. Quercetin and troxerutin share a common core structure; however, in troxerutin, four of the five hydroxyl (-OH) groups of quercetin are blocked, which may influence its metal coordination properties. In this study, we synthesized and fully characterized the VOtroxerutin complex using FTIR, EPR, UV–Vis, and reflectance spectroscopies, along with elemental, thermal, and conductivity analyses. Additionally, we prepared the reported VOquercetin complex, which shares the same coordination sphere as VOtroxerutin, to explore a relationship between the structure of the complexes and their activities. Their anticancer potential was tested through in vitro cytotoxicity assays against the A549 human lung cancer cells and HaCaT normal human keratinocytes. Both complexes exhibited anticancer activities (viability inhibition at 100 μM: 32.1 %, VOtroxerutin; 39.5 %,VOquercetin) and selectivity, highlighting their therapeutic potential. Notably, their pro-oxidant effects were activated upon incubation with cancer cells, leading to oxidative stress-induced cytotoxicity and mitochondrial membrane disruption. Further comparisons with the VOrutin complex provided additional insights into the correlation between anticancer activity and the coordination environment of the VOFlavonoid complexes. Additionally, we evaluated the safety profile of VOtroxerutin, finding no acute toxicity or mutagenic effects, supporting its potential as a targeted anticancer therapy with normal cells viability inhibition only at 100 μM (10 %).</div></div>","PeriodicalId":364,"journal":{"name":"Journal of Inorganic Biochemistry","volume":"268 ","pages":"Article 112915"},"PeriodicalIF":3.8,"publicationDate":"2025-04-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143800407","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) tetrapyrazole-based complex as a new peroxidase-mimetic compound","authors":"Marek Šebela ,&nbsp;Giorgio Zoppellaro ,&nbsp;Zdeněk Trávníček","doi":"10.1016/j.jinorgbio.2025.112911","DOIUrl":"10.1016/j.jinorgbio.2025.112911","url":null,"abstract":"<div><div>A copper(II) tetrapyrazole-based complex of the composition of [Cu(tpyr)(H₂O)(ONO₂)]NO₃ (<strong>1</strong>), where tpyr represents a tetradentate <em>N</em>-donor ligand formed by the condensation of 1<em>H</em>-pyrazole-5-carbaldehyde in NaOH/MeOH medium, has been prepared and characterized by elemental analysis, infrared spectroscopy, ultraviolet-visible spectroscopy, mass spectrometry, electron paramagnetic resonance and single-crystal X-ray diffraction. Spectrophotometric measurements demonstrated a remarkable peroxidase activity of the complex, which utilized hydrogen peroxide for the oxidation of phenolic compounds such as guaiacol or 3,5-dichloro-2-hydroxybenzene sulfonic acid. The optimum conditions for this reaction were found at pH 8 in ammonium bicarbonate buffer, although the activity was low but still detectable at pH 5–6 in ammonium acetate. As a peroxidase mimic, the complex exhibited enzyme-like Michaelis-Menten kinetics, showing a hyperbolic dependence of the reaction rate on hydrogen peroxide concentration. The determined <em>K</em>_m and <em>k</em>_cat values were 651 μmol·l⁻¹ and 6.7 × 10⁻⁴ s⁻¹, respectively, compared to 41 μmol·l⁻¹ and 73 s⁻¹ for horseradish peroxidase. EPR spectroscopy of the reaction mixture revealed no change in the copper (II) oxidation state during catalysis, suggesting that the oxidation of guaiacol may occur simultaneously with the reduction of hydrogen peroxide to water at the copper centre.</div></div>","PeriodicalId":364,"journal":{"name":"Journal of Inorganic Biochemistry","volume":"268 ","pages":"Article 112911"},"PeriodicalIF":3.8,"publicationDate":"2025-04-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143800405","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":"Regulation of ferryl reactivity by the cytochrome P450 decarboxylase OleT","authors":"Hannah E. Gering ,&nbsp;Olivia M. Manley ,&nbsp;Alexis J. Holwerda ,&nbsp;Job L. Grant ,&nbsp;Steven C. Ratigan ,&nbsp;Thomas M. Makris","doi":"10.1016/j.jinorgbio.2025.112912","DOIUrl":"10.1016/j.jinorgbio.2025.112912","url":null,"abstract":"<div><div>The cytochrome P450 OleT catalyzes the decarboxylation of long-chain fatty acid substrates to produce terminal alkenes using hydrogen peroxide as a co-substrate. The facile activation of peroxide to form Compound I in the first step of the reaction, and subsequent C<img>C bond cleavage mediated by Compound II, provides a unique opportunity to visualize both ferryl intermediates using transient kinetic approaches. Analysis of the Arrhenius behavior yields activation barriers of ∼6 kcal/mol and ∼ 18 kcal/mol for the decay of Compound I and Compound II respectively. The influence of the secondary coordination sphere, probed through site-directed mutagenesis approaches, suggests that restriction of the donor-acceptor distance contributes to the reactivity of Compound I. The reactivity of Compound II was further probed using kinetic solvent isotope effect approaches, confirming that the large barrier owes to a proton-gated mechanism in the decarboxylation reaction coordinate. Hydrogen-bonding to an active-site histidine (H85) in the distal pocket plays a key role in this process.</div></div>","PeriodicalId":364,"journal":{"name":"Journal of Inorganic Biochemistry","volume":"270 ","pages":"Article 112912"},"PeriodicalIF":3.8,"publicationDate":"2025-04-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143824267","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":"A highly positively charged Ru(II) complex with photo-labile ligands for selective and efficient photo-inactivation of intracellular Staphylococcus aureus","authors":"Yunli Xu ,&nbsp;Xuwen Da ,&nbsp;Yao Jian ,&nbsp;Wanpeng Zhou ,&nbsp;Aifeng Wu ,&nbsp;Yao Wu ,&nbsp;Yatong Peng ,&nbsp;Xiulian Liu ,&nbsp;Yu Shi ,&nbsp;Xuesong Wang ,&nbsp;Qianxiong Zhou","doi":"10.1016/j.jinorgbio.2025.112908","DOIUrl":"10.1016/j.jinorgbio.2025.112908","url":null,"abstract":"<div><div>Due to the protection afforded by host cells, intracellular <em>Staphylococcus aureus</em> (<em>S. aureus</em>), particularly methicillin-resistant <em>S. aureus</em> (MRSA), poses a significantly greater challenge to eliminate compared to the extracellular counterparts. It is highly desirable to develop novel antibacterial agents which are capable of selectively and efficiently eradicating intracellular bacteria, including drug-resistant strains, while being less prone to induce bacterial resistance. In this work, two Ru(II) complexes (Ru1 and Ru2) with photo-labile ligands were designed and synthesized. Both Ru1 and Ru2 could covalently bind to DNA after photo-induced ligand dissociation. Compared to Ru1, the incorporation of a triphenylamine group adorned with two positively charged cationic pyridine units significantly boosts the DNA binding constant, bacterial binding/uptake level, and subsequently, the antibacterial activity of Ru2. Ru2 could selectively photo-inactivate intracellular <em>S. aureus</em> and MRSA, being more efficient than vancomycin both <em>in vitro</em> and <em>in vivo</em>. Interestingly, after 20 days' treatment at sublethal concentrations, <em>S. aureus</em> cells exhibited no obvious drug resistance towards Ru2 upon irradiation. Such appealing results may provide new sights for developing novel antibacterial agents against intractable intracellular pathogens and also prevalent drug resistance.</div></div>","PeriodicalId":364,"journal":{"name":"Journal of Inorganic Biochemistry","volume":"268 ","pages":"Article 112908"},"PeriodicalIF":3.8,"publicationDate":"2025-04-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143800406","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":"Intrinsically photoluminescent hydrogels to measure peptides‑copper binding affinities","authors":"Alessia Distefano ,&nbsp;Paolo Corsaro ,&nbsp;Nunzio Tuccitto ,&nbsp;Francesca Laneri ,&nbsp;Olivier Monasson ,&nbsp;Elisa Peroni ,&nbsp;Giuseppe Grasso","doi":"10.1016/j.jinorgbio.2025.112914","DOIUrl":"10.1016/j.jinorgbio.2025.112914","url":null,"abstract":"<div><div>NH₂ decorated intrinsically photoluminescent hydrogels (IPH-NH₂) were functionalized with the addition of various peptides via EDC/NHS coupling method. These peptidic devices bind copper with binding affinities depending on surface functionalization. Particularly, fluorescence analysis of copper titrations, alongside the determination of quenching efficiency and lifetime measurements, allowed to assess binding constants and to elucidate the underlying binding mechanism. Various peptides, having the same copper binding amino acidic residues (GHK) but different chain lengths, were tested and it was found that increasing the distance of the GHK sequence from the IPH-NH₂ surface resulted in a decrease in the binding constant, as well as a reduction in quenching efficiency, whereas the binding mechanism remained unchanged as indicated by lifetime measurements. This method not only provides binding constants for peptides immobilized on biosensor surfaces or pre-fabricated devices without altering their structure, but also contributes to the optimization of biosensor design, tailoring it to its intended application.</div></div>","PeriodicalId":364,"journal":{"name":"Journal of Inorganic Biochemistry","volume":"268 ","pages":"Article 112914"},"PeriodicalIF":3.8,"publicationDate":"2025-04-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143791270","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}