Bioorganic Chemistry最新文献

{"title":"Development of thiazole-hydrazone hybrids for targeted therapy of non-small cell lung cancer.","authors":"Mehlika Dilek Altıntop, İpek Ertorun, Gülşen Akalın Çiftçi, Ahmet Özdemir","doi":"10.1016/j.bioorg.2026.110369","DOIUrl":"10.1016/j.bioorg.2026.110369","url":null,"abstract":"<p><p>To identify targeted cytotoxic agents for the treatment of non-small cell lung cancer (NSCLC), novel thiazolyl hydrazones (2a-t) were synthesized and evaluated for their cytotoxicity toward A549 human lung adenocarcinoma and L929 mouse embryonic fibroblast cells. Among these compounds, compound 2b exhibited the highest cytotoxic activity against A549 cells (IC₅₀= 6.10 µM), followed by compounds 2g, 2k, 2r, 2f, 2o, 2e, 2s, and 2h, all of which were more potent than erlotinib (IC₅₀ = 77.35 μM). In vitro mechanistic assays were conducted to assess their effects on apoptosis, cell cycle, epidermal growth factor receptor (EGFR), Akt, and signal transducer and activator of transcription 3 (STAT3). Flow cytometry analyses revealed that these agents induced apoptosis and G0/G1 cell cycle arrest, indicating that their cytotoxic effects are mediated through these mechanisms. Compound 2f was identified as the most promising compound, exhibiting selective cytotoxicity mediated by the concurrent inhibition of EGFR, Akt, and STAT3, with greater inhibitory potency toward EGFR and STAT3 relative to the EGFR TKI erlotinib and the STAT3 inhibitor C188-9. Compound 2e emerged as a potent dual EGFR/STAT3 inhibitor, exerting EGFR inhibitory activity comparable to that of erlotinib while exhibiting superior STAT3 inhibitory activity relative to C188-9. Compound 2b showed the highest cytotoxic potency against A549 cells, primarily through EGFR inhibition, with 8.3-fold greater activity than erlotinib. Compound 2r was identified as the most potent STAT3 inhibitor, exerting 10.8-fold higher activity than C188-9. These findings highlight the potential of thiazolyl hydrazones as targeted therapeutic agents, warranting further investigations for NSCLC treatment.</p>","PeriodicalId":257,"journal":{"name":"Bioorganic Chemistry","volume":"181 ","pages":"110369"},"PeriodicalIF":5.1,"publicationDate":"2026-10-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148786283","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Design, synthesis, and evaluation of aminopyrazolopyrimidopyridone derivatives as RET^V804M and RET^G810C inhibitors based on a \"chemical adaptation\" strategy.","authors":"Jieman Lin, Shuyu Jia, Jianjun Wu, Anzhi Li, Jiaqing Zhu, Yongdong Li, Meipin Liu, Jiayi Shen","doi":"10.1016/j.bioorg.2026.110385","DOIUrl":"10.1016/j.bioorg.2026.110385","url":null,"abstract":"<p><p>Oncogenic conversion of the RET (rearranged during transfection) tyrosine kinase is a well-recognized drug target for cancer treatment. Despite the FDA approval of two selective second-generation RET inhibitors, selpercatinib and pralsetinib, acquired resistance through solvent-front mutations has been identified rapidly. RET^G810 mutations at the solvent front site have been identified as the major on-target mutations contributing to resistance against selpercatinib and pralsetinib. Therefore, the development of next-generation RET inhibitors to overcome acquired solvent-front resistance mutations is urgently needed. In this study, a class of aminopyrazolpyrimidopyridone derivatives, such as RET^V804M gatekeeper mutations and RET^G810C solvent-front mutant inhibitors, were designed and synthesized to overcome resistance to second-generation RET inhibitors. One of the optimal compounds, 11ic, inhibited the proliferation of BaF3 cells harboring the CCDC6-RET^V804M and CCDC6-RET^G810C mutations, with IC₅₀ values of 0.0208 μM and 0.096 μM, respectively. It presented a favorable oral pharmacokinetic profile, with an oral bioavailability of 26.9%, which exceeded that of our previously reported compound. Compound 11ic might be a promising lead compound for the development of novel RET^V804M and RET^G810C inhibitors to overcome clinical acquired resistance.</p>","PeriodicalId":257,"journal":{"name":"Bioorganic Chemistry","volume":"181 ","pages":"110385"},"PeriodicalIF":5.1,"publicationDate":"2026-10-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148786297","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Discovery of a thermostable eugenol oxidase for vanillin biosynthesis from vanillyl alcohol via resting whole-cell catalysis.","authors":"Xi Shen, Ji-Hang Shen, Fu-Lei Liu, Heng Lei, Zhi-Gang Zhang, Xiao-Jun Ji","doi":"10.1016/j.bioorg.2026.110424","DOIUrl":"10.1016/j.bioorg.2026.110424","url":null,"abstract":"<p><p>Bacterial eugenol oxidases (EUGOs) belong to the 4-phenol oxidase subfamily of the VAO/PCMH flavoprotein family and are versatile biocatalysts offering potential for use in biotechnology and organic synthesis. In this work, a thermostable EUGO from Capillimicrobium sp. (CsEUGO) was identified and overexpressed in E. coli cells as a whole-cell biocatalyst for the biosynthesis of vanillin from vanillyl alcohol. The E. coli-CsEUGO cells oxidized vanillyl alcohol aerobically, producing only vanillin, indicating excellent reaction selectivity. Furthermore, the cells retained 63% and 57% of their activity after 6 and 12 h at 40 °C, and 40% of their activity at 50 °C. Under optimal reaction conditions, the cells converted a 200 mM concentration of substrate to vanillin, with a yield of 93%. With a fed-batch feeding method, a total of 208 mM vanillin was produced, affording a productivity of 1.0 g L^-1 h^-1 and a yield of 83%. Furthermore, it was found that the E. coli-CsEUGO whole-cell biocatalyst is active on several phenolic substrates, indicating a broad catalytic substrate scope. The research highlights a new biocatalyst that can selectively oxidize vanillyl alcohol, leading to the production of value-added vanillin. Additionally, it is applicable for catalytic hydroxylation, oxidative deamination, and dehydrogenation in organic synthesis.</p>","PeriodicalId":257,"journal":{"name":"Bioorganic Chemistry","volume":"181 ","pages":"110424"},"PeriodicalIF":5.1,"publicationDate":"2026-10-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148808185","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Radioiodination, biological distribution, and docking study of diosmetin as a potential radiotracer for infection detection.","authors":"Safaa B Challan, S I Khater, Hossam M Hassan, Mostafa A Mansour, Dina M El-Sharawy","doi":"10.1016/j.bioorg.2026.110400","DOIUrl":"10.1016/j.bioorg.2026.110400","url":null,"abstract":"<p><p>Staphylococcus aureus infections, particularly methicillin-resistant strains, pose major diagnostic challenges in differentiating septic from aseptic inflammation. This study aimed to radiolabel diosmetin (3',5,7-trihydroxy-4'-methoxyflavone), a natural flavonoid with antibacterial and anti-inflammatory properties, with iodine-131 (¹³¹I) and to evaluate its potential as a radiotracer for infection imaging. Diosmetin was isolated from Rosmarinus officinalis and radiolabeled with Na¹³¹I using the chloramine-T method. The radiochemical yield (RCY), and stability were assessed using TLC/HPLC. Molecular docking to COX-2 (PDB: 5KIR) was performed using the MOE software. In vitro binding to S. aureus was measured, and biodistribution studies were conducted in normal, inflamed, and infected Swiss Albino mice (n = 7 per subgroup) at 0.5-3 h post-injection. Target-to-non-target (T/NT) ratios were calculated from the %ID/g values. Radiolabeling achieved 95.8 ± 0.12% yield with >3 h of stability in PBS and serum. Docking revealed a strong COX-2 affinity. In vitro binding to S. aureus reached 52 ± 1.5%. In infected mice, [¹³¹I]DSM accumulated selectively in the infected muscle (3.85 ± 0.10%ID/g at 2 h), yielding a T/NT ratio of 7.7, which was double that in inflamed tissue (3.7). Rapid blood clearance, predominant renal excretion, and low thyroid uptake confirmed the in vivo stability. [¹³¹I]Diosmetin was prepared with high yield and stability, demonstrated selective uptake at infectious foci, and enabled clear differentiation between septic and aseptic inflammation. These findings support its potential as a promising radiotracer for infection imaging applications.</p>","PeriodicalId":257,"journal":{"name":"Bioorganic Chemistry","volume":"181 ","pages":"110400"},"PeriodicalIF":5.1,"publicationDate":"2026-10-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148786418","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Chitosan-PLGA biopolymeric nanogel as a platform for enhanced methotrexate delivery and redox-modulated anti-inflammatory activity.","authors":"Reem Darwesh, Sarah Alharthi, Nora Hamad Al-Shaalan, Mohamed Mohamady Ghobashy, Fatima M Shaaban, Amal M Hammad, Ehab M Zayed, Rasha E Hassan, Ghadah Alrabghi, Ahmad S Kodous","doi":"10.1016/j.bioorg.2026.110412","DOIUrl":"10.1016/j.bioorg.2026.110412","url":null,"abstract":"<p><p>Methotrexate (MTX) is an effective disease-modifying antirheumatic drug for the treatment of chronic inflammatory disorders; however, its clinical application is limited by poor bioavailability, rapid systemic clearance, and dose-dependent adverse effects. In this study, a pH-responsive methotrexate-loaded chitosan/poly(lactic-co-glycolic acid) ((Chit/PLGA)/MTX) nanogel was developed to improve drug delivery and therapeutic performance. The nanogel was fabricated by ionic gelation followed by gamma radiation-induced in situ free-radical polymerization (20 kGy) and subsequently loaded with methotrexate using a pH-triggered swelling-shrinking encapsulation strategy. Physicochemical characterization by TEM, DLS, FTIR, UV-Vis spectroscopy, and zeta potential analysis confirmed the successful formation of spherical nanogel particles with an average hydrodynamic diameter of 125 nm, a polydispersity index of 0.18 ± 0.03, and a zeta potential of -2.5 mV. The nanogel exhibited a high encapsulation efficiency (89.3 ± 2.1%) and drug-loading capacity (15.1 ± 0.8%). In vitro release studies demonstrated pronounced pH-responsive behavior, with cumulative methotrexate release reaching approximately 60% at pH 5.5 compared with 40% at pH 7.4 after 300 s, indicating preferential drug release under acidic inflammatory conditions. Cytotoxicity evaluation showed that the nanogel formulation exhibited improved biocompatibility (IC₅₀ = 422.5 μg/mL) compared with free methotrexate (IC₅₀ = 311.7 μg/mL). The (Chit/PLGA)/MTX nanogel significantly enhanced antioxidant activity, exhibiting 79.1% DPPH radical scavenging, 81.8% membrane stabilization, and 83.3% inhibition of protein denaturation. Furthermore, the formulation effectively suppressed the expression of major inflammatory mediators, including COX-2 (37.2%), iNOS (47.2%), TNF-α (40.3%), and NF-κB (40.9%), while reducing IL-1β (33.5%) and IL-6 (45.0%) production. Collectively, these findings demonstrate that the pH-responsive Chitosan-PLGA nanogel provides efficient methotrexate encapsulation, controlled drug release, enhanced antioxidant activity, and potent anti-inflammatory effects, highlighting its promise as a nanocarrier platform for the treatment of chronic inflammatory diseases.</p>","PeriodicalId":257,"journal":{"name":"Bioorganic Chemistry","volume":"181 ","pages":"110412"},"PeriodicalIF":5.1,"publicationDate":"2026-10-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148838696","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Design, synthesis, and biological evaluation of novel furo[3,2-b]pyrrole-benzimidazole series as potential protein tyrosine phosphatase (PTPs) inhibitors.","authors":"Slieman Milaneh, Zehao Ye, Li-Xing Gao, Jia Li, Yu-Bo Zhou, Lei Xu, Wen-Long Wang","doi":"10.1016/j.bioorg.2026.110373","DOIUrl":"10.1016/j.bioorg.2026.110373","url":null,"abstract":"<p><p>Protein tyrosine phosphatases (PTPs) are essential for regulating cell signaling pathways, and their dysregulation is linked to various human diseases, including cancer and diabetes, making them important therapeutic targets. However, developing PTP inhibitors remains challenging due to the conserved structure and charged active sites. In this study, a series of furo[3,2-b]pyrrole-benzimidazole derivatives was designed and synthesized as potential PTP inhibitors. Structure-activity relationship (SAR) studies showed that extending the aromatic system with the benzimidazole scaffold increased potency, and the carboxylic acid group was essential for inhibitory activity. Among the synthesized compounds, 5a was identified as the lead compound, exhibiting strong inhibitory activity against PTP1B (IC₅₀ = 0.70 ± 0.04 μM) and the oncogenic SHP2-E76K mutant (IC₅₀ = 0.36 ± 0.02 μM). Molecular docking studies suggest that the inhibitory activity of this series may depend on the compounds' ability to bind a putative allosteric site, thereby stabilizing the WPD loop in its inactive, open conformation; kinetic and biophysical validation of this mechanism is planned for future work. Antiproliferative cell tests demonstrated that although compound 5a exhibited superior enzymatic inhibition, smaller analogs, such as 2a, lacking the extended benzimidazole moiety, showed more potent, dose-dependent cytotoxicity in U2OS human osteosarcoma cells (IC₅₀ = 16.25 μM vs. 157.24 μM for 5a), likely due to improved physicochemical properties and membrane permeability. These findings offer a promising scaffold for future development and optimization of potent, broad-drug-like PTP inhibitors with enhanced activity against the full-length SHP2-E76K construct relative to the isolated catalytic domains tested.</p>","PeriodicalId":257,"journal":{"name":"Bioorganic Chemistry","volume":"181 ","pages":"110373"},"PeriodicalIF":5.1,"publicationDate":"2026-10-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148786303","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Discovery and characterization of pyridazino[4,5-b]indol-4-one derivatives as Na_V1.8 inhibitors: A novel approach for targeting chronic pain.","authors":"Shilong Hu, Gen Li, Runduo Liu, Di Zhang, Wencheng Liu, Shouwei Tao, Zhuang Miao, Zhe Li, Bowen Ke","doi":"10.1016/j.bioorg.2026.110375","DOIUrl":"10.1016/j.bioorg.2026.110375","url":null,"abstract":"<p><p>Voltage-gated sodium channel Na_V1.8 plays a key role in the development and progression of neuropathic and inflammatory pain, making it an important target for chronic pain treatment. However, the development of drugs targeting Na_V1.8 and other ion channels is still constrained by the low throughput and high cost of conventional patch-clamp techniques. Additionally, existing Na_V1.8 inhibitors suffer from structural uniformity, poor analgesic activity and unfavorable pharmacokinetic properties. In this study, we built a customized virtual screening workflow that combines the structural features of the Na_V1.8 binding pocket with large-scale molecular docking, and applied absolute binding free energy (ABFE) calculations to improve both accuracy and efficiency. Using cell membrane chromatography (CMC) combined with whole-cell patch-clamp assays, we identified compound 12 as a lead compound with potent inhibitory activity against Na_V1.8. Based on compound 12, 17 derivatives were synthesized, and compound 12d was identified as the most promising one after a series of in vitro and in vivo evaluations. This study not only provides a promising lead compound for chronic pain therapy but also offers a paradigm for the precise design and development of drugs targeting other ion channels.</p>","PeriodicalId":257,"journal":{"name":"Bioorganic Chemistry","volume":"181 ","pages":"110375"},"PeriodicalIF":5.1,"publicationDate":"2026-10-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148786371","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Green synthesis of N-aryl-1-(2-bromo-4-methyl phenyl)-1H-tetrazol-5-amines as novel anti-cancer agents targeting tubulin-Combretastatin A4 complex and human non-small cell lung cancer cell lines.","authors":"Uma Ravi Sankar Arigala, Raju Vasantham, Santhosh Kumar Nadikatla, Ibrahim Khalivulla Shaik, Yellappa Masapogu","doi":"10.1016/j.bioorg.2026.110410","DOIUrl":"10.1016/j.bioorg.2026.110410","url":null,"abstract":"<p><p>A series of N-aryl-1-(2-bromo-4-methyl phenyl)-1H-tetrazol-5-amines was synthesized through a two-step microwave-assisted protocol from 2-bromo-1-isothiocyanato-4-methylbenzene and substituted aryl amines. Initially, thiourea derivatives were prepared under solvent-free microwave conditions, followed by cyclization with sodium azide in the presence of potassium hydroxide and molecular iodine to afford the desired tetrazole derivatives in good to excellent yields within short reaction times. All synthesized compounds were characterized by FT-IR, ¹H NMR, ¹³C NMR, and mass spectral analysis. The anti-lung cancer activity of compounds was evaluated against A549, EKVX, and NCI-H460 cell lines. Compounds substituted with isopropyl and benzo[d][1,3]dioxole exhibited the most potent anti-proliferative activity compared to the reference drug Combretastatin A4. Molecular docking studies against tubulin protein (PDB ID: 5LYJ) revealed favorable binding interactions within the colchicine binding pocket, mainly involving GLU22 amino acid residue. Furthermore, ADMET, QSAR, bioactivity, toxicity risk, drug property and molecular fingerprint property evaluation studies indicated favorable drug-like properties, good absorption characteristics, and non-toxic nature of the synthesized compounds. Overall, the present study identifies tetrazole derivatives as promising scaffolds for the development of potential anti-lung cancer agents.</p>","PeriodicalId":257,"journal":{"name":"Bioorganic Chemistry","volume":"181 ","pages":"110410"},"PeriodicalIF":5.1,"publicationDate":"2026-10-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148786398","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Short chain length polyhydroxyalkanoate (scl-PHA) produced by the marine bacterium Pseudomonas sputi MaRe06 inhibits Staphylococcus aureus biofilm formation.","authors":"Leidy J García Maza, Deisiane Da Rosa, Walter O Beys-da-Silva, Lucélia Santi, Augusto Schrank, Marilene Henning Vainstein, Alexandre J Macedo","doi":"10.1016/j.bioorg.2026.110431","DOIUrl":"10.1016/j.bioorg.2026.110431","url":null,"abstract":"<p><p>Staphylococcus aureus is a major biofilm-forming pathogen that is often linked to skin infections and colonization of medical devices. This bacterium poses a significant challenge to infection control efforts. This study isolated and characterized a short chain length polyhydroxyalkanoate (scl-PHA) produced by the marine bacterium Pseudomonas sputi MaRe06 as an antibiofilm agent. Structural characterization using FT-IR, ESI-TOF MS and ¹H NMR revealed a copolymer composed of hydroxybutyrate (HB) and hydroxyvalerate (HV) units, corresponding to poly(3-hydroxybutyrate-co-3-hydroxyvalerate) [poly(3HB-co-3 HV)]. ESI+ and ESI- mass spectra showed oligomeric distributions consistent with HB/HV combinations. The PHA exhibited strong antibiofilm activity against S. aureus, reaching 92% inhibition at 300 μg/mL. Using the Galleria mellonella in vivo model, toxicity evaluation showed 83.33% larvae survival at 50 mg/kg, with no significant difference compared to viability controls (two-way ANOVA, Bonferroni test, p < 0.05). To our knowledge, this is the first report of poly(3HB-co-3 HV) production by Pseudomonas sputi and the first evaluation of the antibiofilm potential of scl-co-PHA from this marine species isolated from restinga ecosystems. These findings highlight P. sputi MaRe06 as a promising microbial platform for producing bioactive compounds capable of inhibiting bacterial biofilm formation.</p>","PeriodicalId":257,"journal":{"name":"Bioorganic Chemistry","volume":"181 ","pages":"110431"},"PeriodicalIF":5.1,"publicationDate":"2026-10-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148816977","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Corrigendum to \"Discovery of a novel twin drug from Phillygenin and glucosamine for osteoarthritis treatment\" [Bioorg. Chem. 181 (2026) 110327].","authors":"Jiajing Zhang, Xinxin Lv, Yicong Sun, Jie Lu, Guangwei Cui, Guangfu Sun, Xiaobei Chen, Huan Xu, Yongqiang Zhang","doi":"10.1016/j.bioorg.2026.110428","DOIUrl":"10.1016/j.bioorg.2026.110428","url":null,"abstract":"","PeriodicalId":257,"journal":{"name":"Bioorganic Chemistry","volume":" ","pages":"110428"},"PeriodicalIF":5.1,"publicationDate":"2026-10-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148856832","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}