Bioorganic & Medicinal Chemistry最新文献

{"title":"Quantitative and site-specific chemoproteomic profiling of O-GlcNAcylation in Drosophila","authors":"Cong Lei ,&nbsp;Zihan Chen ,&nbsp;Yi Hao ,&nbsp;Wanping Huang ,&nbsp;Tianyu Chu ,&nbsp;Kangming Xiao ,&nbsp;Che Zhang ,&nbsp;Wen Zhou ,&nbsp;Chenjian Li ,&nbsp;Xing Chen","doi":"10.1016/j.bmc.2025.118191","DOIUrl":"10.1016/j.bmc.2025.118191","url":null,"abstract":"<div><div>Protein O-GlcNAcylation plays a crucial role in <em>Drosophila melanogaster</em> development. Dysregulation of O-GlcNAc transferase (<em>sxc</em>/<em>Ogt</em>) and O-GlcNAcase (<em>Oga</em>) disrupts early embryogenesis and locomotor behavior. It is therefore of great interest to identify and quantitatively analyze O-GlcNAcylation sites in <em>Drosophila</em>. Here, we perform quantitative and site-specific profiling of O-GlcNAcylation in <em>Drosophila</em> by employing a chemoenzymatic labeling strategy. A total of 2196 unambiguous O-GlcNAcylation sites and 1308 O-GlcNAcylated proteins are identified. Quantitative analysis of O-GlcNAcylation in the head of <em>Drosophila</em> with <em>sxc</em>/<em>Ogt</em> knockdown in GABAergic neurons reveals a reduction in O-GlcNAcylation of several proteins involved in muscle development, consistent with the phenotypic defects observed in <em>sxc</em>/<em>Ogt</em> RNAi <em>Drosophila</em>. Furthermore, quantitative analysis of O-GlcNAcylation under a high-sugar diet reveals altered O-GlcNAcylation of several proteins associated with obesity and neurological diseases, such as Hex-A and Ankyrin 2. Our study not only establishes an effective method for large-scale identification of O-GlcNAcylation sites, but also provides a valuable resource for studying O-GlcNAc biology in <em>Drosophila</em>.</div></div>","PeriodicalId":255,"journal":{"name":"Bioorganic & Medicinal Chemistry","volume":"124 ","pages":"Article 118191"},"PeriodicalIF":3.3,"publicationDate":"2025-04-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143834797","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Truncated pyridinylbenzylamines: Potent, selective, and highly membrane permeable inhibitors of human neuronal nitric oxide synthase","authors":"Dhananjayan Vasu ,&nbsp;Ha T. Do ,&nbsp;Huiying Li ,&nbsp;Christine D. Hardy ,&nbsp;Thomas L. Poulos ,&nbsp;Richard B. Silverman","doi":"10.1016/j.bmc.2025.118193","DOIUrl":"10.1016/j.bmc.2025.118193","url":null,"abstract":"<div><div>Neuronal nitric oxide synthase (nNOS) is a promising target for addressing various neurological disorders and melanoma. Our discovery of a series of truncated pyridinylbenzylamines has yielded potent, selective, and membrane permeable inhibitors of human neuronal nitric oxide synthase. By implementing an efficient synthetic procedure using the Suzuki–Miyaura cross-coupling reaction, we were able to rapidly identify a potent inhibitor. This new inhibitor (<strong>18</strong>, 6-(2,3-difluoro-5-((methylamino)methyl)phenyl)-4-methylpyridin-2-amine dihydrochloride) exhibits excellent potency, with <em>K</em>_i values of 30 nM for human nNOS and 40 nM for rat nNOS. It also demonstrates high isoform selectivity, showing an 821-fold preference for human nNOS over human endothelial NOS (eNOS) and a 75-fold selectivity over human inducible NOS (iNOS). Additionally, inhibitor <strong>18</strong> displays high permeability (<em>P</em>_e = 10.7 × 10⁻⁶ cm s⁻¹) in an artificial membrane permeability assay. The crystal structures of several NOS-inhibitor complexes provide valuable structural insights into the potency and selectivity of this series of novel inhibitors. A particularly notable finding is the unexpected role of a Cl⁻ anion bound to heNOS, which contributes to the high isoform selectivity of these inhibitors and explains why heNOS binds Cl⁻, while hnNOS does not. This unique Cl⁻ binding site could be important in future inhibitor design, opening new avenues for the development of more selective NOS inhibitors. Additionally, the presented crystal structures reveal the key factors required to maintain both high potency and selectivity in the simplified inhibitors discussed in this study.</div><div>Abbreviations: NO, nitric oxide; nNOS, neuronal nitric oxide synthase; iNOS, inducible nitric oxide synthase; eNOS, endothelial nitric oxide synthase; rnNOS, rat neuronal nitric oxide synthase; hnNOS, human neuronal nitric oxide synthase; hiNOS, human inducible nitric oxide synthase; heNOS, human endothelial nitric oxide synthase; <span>l</span>-Arg, <span>l</span>-arginine; NADPH, reduced nicotinamide adenine dinucleotide phosphate; CaM, calmodulin; H₄B, (6<em>R</em>)-5,6,7,8-tetrahydrobiopterin; FAD, flavin adenine dinucleotide; FMN, Flavin mononucleotide, BBB, blood–brain barrier; CNS, central nervous system; PAMPA, parallel artificial membrane permeability assay; P-gp, P-glycoprotein; ER, efflux ratio; <em>P</em>_e, effective permeability; <em>P</em>_app, apparent permeability; Caco-2, cancer coli-2; TLC, thin layer chromatography; TBAF, tetra-<em>n</em>-butylammonium fluoride; TFA, trifluoroacetic acid.</div></div>","PeriodicalId":255,"journal":{"name":"Bioorganic & Medicinal Chemistry","volume":"124 ","pages":"Article 118193"},"PeriodicalIF":3.3,"publicationDate":"2025-04-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143845057","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Development of GluN2A NMDA receptor positive allosteric modulators: Recent advances and perspectives","authors":"Ping Li ,&nbsp;Jiacheng Wang ,&nbsp;Mengjiao Wang ,&nbsp;Xin Chen ,&nbsp;Hongyu Zhu ,&nbsp;Mingxin Dong","doi":"10.1016/j.bmc.2025.118194","DOIUrl":"10.1016/j.bmc.2025.118194","url":null,"abstract":"<div><div><em>N</em>-methyl-<span>d</span>-aspartate (NMDA) receptors, functioning as glutamate-gated ion channels, mediate the permeation of Ca²⁺ and are essential for excitatory synaptic transmission and synaptic plasticity within the central nervous system (CNS). During brain development, there is a switch from an early dominance of GluN2B subunit expression to the incorporation of GluN2A subunits at mature synapses. NMDARs hypofunction is implicated in various psychiatric disorders, and activation of NMDARs containing GluN2A has recently attracted attention as a promising therapeutic approach for treating these diseases. This review focuses on the selective positive allosteric modulators (PAMs) that specifically target the ligand-binding domain (LBD) and <em>N</em>-terminal domain (NTD) regions of GluN2A subtype, as well as non-subunit selective PAMs, and discusses their implications in neuropsychiatric diseases such as stroke, depression, Alzheimer’s disease, and Huntington’s disease.</div></div>","PeriodicalId":255,"journal":{"name":"Bioorganic & Medicinal Chemistry","volume":"124 ","pages":"Article 118194"},"PeriodicalIF":3.3,"publicationDate":"2025-04-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143834861","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Construction of 3-oxo-3H-spiro[benzofuran-2,1′-cyclopentane] carboxylic acid derivatives via phosphine-catalyzed [4 + 1] annulations and their biological evaluation against fibrosis","authors":"Sheng-Hong Li ,&nbsp;Feng-Yi Lu ,&nbsp;Muralikrishna Katta,&nbsp;Yun-Yun Liu,&nbsp;Danling Huang,&nbsp;Yong-Xian Cheng","doi":"10.1016/j.bmc.2025.118192","DOIUrl":"10.1016/j.bmc.2025.118192","url":null,"abstract":"<div><div>A novel phosphine-catalyzed [4 + 1] cyclization reaction was developed to construct the 3-oxo-3<em>H</em>-spiro[benzofuran-2,1′-cyclopentane] scaffold. Utilizing this innovative method, twenty diverse 3-oxo-3<em>H</em>-spiro[benzofuran-2,1′-cyclopentane] carboxylic acid derivatives were synthesized and evaluated for their anti-fibrotic activities. Compound <strong>L10-P1</strong> possessed potential anti-fibrotic activity by inhibiting the expression of fibronectin, collagen I, and α-SMA. This study presents a new synthetic route for 3<em>H</em>-spiro[benzofuran-2,1′<em>-</em>cyclopentan]-3-one derivatives, contributing valuable insights into the chemical and biological diversity of these compounds.</div></div>","PeriodicalId":255,"journal":{"name":"Bioorganic & Medicinal Chemistry","volume":"124 ","pages":"Article 118192"},"PeriodicalIF":3.3,"publicationDate":"2025-04-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143845077","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"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 Implications of Autotaxin inhibitors with a Three-Point lock binding mode","authors":"Nicolas Desroy ,&nbsp;Razvan Borza ,&nbsp;Jörg Heiermann ,&nbsp;Nicolas Triballeau ,&nbsp;Agnès Joncour ,&nbsp;Natacha Bienvenu ,&nbsp;Willem Jan Hengeveld ,&nbsp;Jasper Springer ,&nbsp;René Galien ,&nbsp;Robbie P. Joosten ,&nbsp;Anastassis Perrakis ,&nbsp;Bertrand Heckmann","doi":"10.1016/j.bmc.2025.118181","DOIUrl":"10.1016/j.bmc.2025.118181","url":null,"abstract":"<div><div>Autotaxin (ATX) is a circulating enzyme that plays a major role in the production of the signaling mediator lysophosphatidic acid (LPA). A role for ATX/LPA signaling has been described in multiple disease areas, including fibrosis and cancer. ATX inhibitors are classified in five types (I-V) depending on how they target parts of the tripartite site (active site, pocket and tunnel). We set to explore a “penultimate” type of inhibitors, targeting all these three parts at once. Designing new analogs extending on an ethyl group of the type IV GLPG1690 compound, yielded potent new molecules. Co-crystal structures confirmed compounds that utilize a three-point lock binding mode. The most potent “type VI” inhibitors, <strong>4</strong> and <strong>41</strong>, displayed increased inhibitory activity (∼40-fold) compared to the type IV close analog <strong>3</strong>. Type VI inhibitors <strong>4</strong> and <strong>41</strong> showed cellular and phenotypic activity similar to type IV inhibitor GLPG1690. Identification of this new binding mode completes this combinatorial puzzle in inhibitor design and calls for further investigation to characterize potential therapeutic benefit.</div></div>","PeriodicalId":255,"journal":{"name":"Bioorganic & Medicinal Chemistry","volume":"124 ","pages":"Article 118181"},"PeriodicalIF":3.3,"publicationDate":"2025-04-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143826119","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Design and identification of brain-penetrant, potent, and selective 1,3-oxazole-based cholesterol 24-hydroxylase (CH24H) inhibitors","authors":"Yoshiteru Ito ,&nbsp;Eiji Kimura ,&nbsp;Izumi Nomura ,&nbsp;Etsurou Watanabe ,&nbsp;Jason Yano ,&nbsp;Robert Skene ,&nbsp;Maki Miyamoto ,&nbsp;Tsuyoshi Ishii ,&nbsp;Toshiya Nishi ,&nbsp;Tatsuki Koike","doi":"10.1016/j.bmc.2025.118182","DOIUrl":"10.1016/j.bmc.2025.118182","url":null,"abstract":"<div><div>Azole-, pyridine-, and pyrimidine-based cytochrome P450 (CYP) inhibitors strongly bind to CYP enzymes through the coordination between the heme iron of CYP and the sp2-nitrogen atoms of heteroaromatic rings, providing potent pharmacological effects by inhibiting the initiation of the catalytic cycles of target CYP enzymes. Although imidazole-, 1,2,4-triazole-, pyridine-, and pyrimidine-based CYP inhibitors have been widely explored, 1,3-oxazole-based CYP inhibitors have received little attention. In this study, we designed and identified novel 1,3-oxazole-based inhibitors of cholesterol 24- hydroxylase (CH24H; CYP46A1), a brain-specific enzyme involved in cholesterol catabolism, to form 24S-hydroxycholesterol. Detailed insights into the CH24H–ligand interactions were provided by the crystal structures of 1,3-oxazole compounds, including high-throughput screening hit 2 and rationally designed inhibitor 3f. Optimization of 3f led to the identification of 1,3-oxazole derivative 4 l as a potent, selective, and brain-penetrable CH24H inhibitor that significantly reduced 24HC levels in the mouse brain. The design of 1,3-oxazole-based CYP inhibitors holds the potential for the discovery of novel inhibitors with significant potency against a broad spectrum of CYP enzymes.</div></div>","PeriodicalId":255,"journal":{"name":"Bioorganic & Medicinal Chemistry","volume":"124 ","pages":"Article 118182"},"PeriodicalIF":3.3,"publicationDate":"2025-04-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143815273","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Brief analysis of Nav1.7 inhibitors: Mechanism of action and new research trends","authors":"Zhoujun Dong ,&nbsp;Baichen Xiong ,&nbsp;Tianyu Sun ,&nbsp;Ruijia Jiang ,&nbsp;Feng Feng ,&nbsp;Haopeng Sun","doi":"10.1016/j.bmc.2025.118180","DOIUrl":"10.1016/j.bmc.2025.118180","url":null,"abstract":"<div><div>Na_v1.7 has been the most studied ion channel among the 9 subtypes of sodium ion, and it is also one of the popular analgesic targets in recent years. Compared with opioid receptors, because of its advantages of targeting a variety of pain types and being unrelated to addiction, many related inhibitors have been excavated for it, including old drugs and new uses, peptides, and new skeleton small molecules. Some of these inhibitors have reached the second phase of clinical research, and some are still in the laboratory research stage. So far, no exclusive Na_v1.7 inhibitor has successfully passed the third phase of clinical research and entered the field of vision of patients. This article reviews the action sites and mechanisms of different Na_v1.7 inhibitors in terms of historical background and related analgesic activities, and also summarizes the related inhibitors that are currently under active development, hoping to provide useful information for the research of new Na_v1.7 inhibitors.</div></div>","PeriodicalId":255,"journal":{"name":"Bioorganic & Medicinal Chemistry","volume":"128 ","pages":"Article 118180"},"PeriodicalIF":3.3,"publicationDate":"2025-04-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144106149","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Alchemical free energy-based optimization of quinazoline derivatives as potent EGFR inhibitors with cytotoxic activity","authors":"U. Martínez-Ortega ,&nbsp;R. Aguayo-Ortiz ,&nbsp;D. Aguilar-Cazares ,&nbsp;E.D. Guerrero-Molina ,&nbsp;V. Aguilar-Martínez ,&nbsp;A. Moreno-Rodríguez ,&nbsp;J.S. López-González ,&nbsp;J.M. Vázquez-Ramos ,&nbsp;F. Hernández-Luis","doi":"10.1016/j.bmc.2025.118179","DOIUrl":"10.1016/j.bmc.2025.118179","url":null,"abstract":"<div><div>Gefitinib (GFB) is a well-established EGFR inhibitor used in the treatment of non-small cell lung cancer (NSCLC) that has shown resistance in certain cases of this cancer. In this work, we aimed to enhance GFB’s inhibitory activity using alchemical free energy calculations, leading to the design of five new quinazoline derivatives. Among these, compound <strong>8a</strong> was the most potent, inhibiting EGFR at 10 µM and showing significant antiproliferative effects at 25 µM. Further optimization identified two new compounds, <strong>NCU00</strong> and <strong>NCU01</strong>, with improved EGFR inhibition and superior cytotoxicity in four NSCLC cell lines compared to GFB. Molecular dynamics simulations revealed crucial interactions that contribute to the enhanced inhibitory activity of <strong>NCU00</strong> and <strong>NCU01</strong>. Toxicological assessments in mice showed no adverse effects on kidney or liver function, and <strong>NCU01</strong> exhibited no developmental toxicity in zebrafish embryos. This study highlights the effectiveness of alchemical free energy methods in optimizing quinazoline-bearing EGFR inhibitors.</div></div>","PeriodicalId":255,"journal":{"name":"Bioorganic & Medicinal Chemistry","volume":"124 ","pages":"Article 118179"},"PeriodicalIF":3.3,"publicationDate":"2025-04-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143785995","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Chemical modification of monensin as a source of potent antiplasmodial agents","authors":"Michał Sulik ,&nbsp;Eyob A. Workneh ,&nbsp;Sofia Santana ,&nbsp;Bárbara Teixeira ,&nbsp;Miguel Prudêncio ,&nbsp;Jan Janczak ,&nbsp;Adam Huczyński","doi":"10.1016/j.bmc.2025.118177","DOIUrl":"10.1016/j.bmc.2025.118177","url":null,"abstract":"<div><div>Malaria remains a significant public health issue and one of the leading causes of child mortality worldwide. Due to the growing problem of drug resistance, new modes of fighting the disease are searched for. In this context, ionophore antibiotics, natural compounds with high potential for combating parasitic diseases, deserve special attention. The primary representative of such compounds, monensin (<strong>MON</strong>), demonstrates exceptionally high antiplasmodial activity. In this work, the C26-amino derivative of <strong>MON</strong> was used as a convenient substrate for the synthesis of its acyl analogues, such as amides and urea. All derivatives exhibited strong activity against the hepatic stage of <em>Plasmodium berghei</em> infection <em>in vitro</em>, which exceeded that shown by the reference drug primaquine. The IC₅₀ value for <strong>MON</strong> <em>O</em>-phenyl urethane (<strong>8</strong>) was less than 1 nM.</div></div>","PeriodicalId":255,"journal":{"name":"Bioorganic & Medicinal Chemistry","volume":"123 ","pages":"Article 118177"},"PeriodicalIF":3.3,"publicationDate":"2025-03-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143769013","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"A novel cinnamic acid derivative for hepatocellular carcinoma therapy by degrading METTL16 protein","authors":"Mingyang Liu ,&nbsp;Muyan Ke ,&nbsp;Hongchen Lu ,&nbsp;Ziyu Feng ,&nbsp;Kaixuan Wang ,&nbsp;Danyang Wang ,&nbsp;Kun Wang ,&nbsp;Yueping Bai ,&nbsp;Song Yang ,&nbsp;Lu Miao ,&nbsp;Qiang Chen ,&nbsp;Mingming Sun ,&nbsp;Changliang Shan ,&nbsp;Jiancheng Hu ,&nbsp;Lingyu Jiang ,&nbsp;Hongzhen Jin ,&nbsp;Jinfang Hu ,&nbsp;Changjiang Huang ,&nbsp;Rui Wang ,&nbsp;Wei Zhao ,&nbsp;Fan Yu","doi":"10.1016/j.bmc.2025.118178","DOIUrl":"10.1016/j.bmc.2025.118178","url":null,"abstract":"<div><div>The RNA methyltransferase methyltransferaselike protein 16 (METTL16) is upregulated in a large proportion of hepatocellular carcinoma (HCC), and its high expression is associated with poor clinical outcomes. METTL16 deletion inhibits HCC growth <em>in vitro</em> and <em>in vivo</em>. Referencing the structure of cinnamic acid, here we designed and synthesized a novel series of small molecular compounds, and found through bioactivity screening that compound <strong>15a</strong> effectively reduced METTL16 level and modulated oncogenic PI3K/AKT pathway signaling. Compound <strong>15a</strong> inhibited the proliferation and migration of HepG2 cells, and induced apoptosis <em>in vitro</em>. Furthermore, compound <strong>15a</strong> significantly inhibited the growth of patient-derived HCC xenografts in nude mice with greater efficacy than the multi-kinase inhibitor lenvatinib. The promising efficacy and good biosafety profile of compound <strong>15a</strong> enables us to further develop this compound for treating patients with HCC and possibly other cancers in clinic.</div></div>","PeriodicalId":255,"journal":{"name":"Bioorganic & Medicinal Chemistry","volume":"124 ","pages":"Article 118178"},"PeriodicalIF":3.3,"publicationDate":"2025-03-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143769137","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}