Bioorganic & Medicinal Chemistry Letters最新文献

{"title":"Design, synthesis, and activity evaluation of indole derivatives as potential stabilizers for p53 Y220C","authors":"Linquan Li ,&nbsp;Xi Gu ,&nbsp;Jingyi Meng ,&nbsp;Yiming Wen ,&nbsp;Jing Yi ,&nbsp;Fengqian Xu ,&nbsp;Li Zhang ,&nbsp;Sulin Zhang ,&nbsp;Zhili Zuo","doi":"10.1016/j.bmcl.2025.130161","DOIUrl":"10.1016/j.bmcl.2025.130161","url":null,"abstract":"<div><div>The p53 Y220C mutation is frequently observed in human cancers. This mutation renders the p53 Y220C unstable at physiological temperatures, leading to a loss of its normal function and promoting tumor development. In this study, a total of eight compounds were designed and synthesized based on the active compound <strong>C8</strong>. The protein thermal shift assay revealed that both <strong>C8-3b</strong> and <strong>C8–6</strong> exhibited similar activity of <strong>C8</strong>, with a ΔT_m value of +0.5 °C. Compounds <strong>C8-1a</strong>, <strong>C8-1b</strong>, and <strong>C8-2b</strong> were found to enhance the thermostability of p53 Y220C (ΔT_m: + 1.0 °C), the melting temperature exhibits an enhancement of 0.5 °C over the <strong>C8</strong>, indicating that these compounds possess the ability to stabilize p53 Y220C. The results of the cell viability assay revealed that <strong>C8-1b</strong> exhibited selective inhibitory effects on the proliferation of tumor cells harboring the p53 Y220C mutation. Furthermore, we utilized molecular docking and two-dimensional interaction analysis to elucidate the binding mode and key interactions of these compounds with p53 Y220C. Our study suggests that these compounds could potentially serve as lead compounds for enhancing the stability of p53 Y220C, thus providing a rational approach for designing small molecule stabilizers against p53 mutations.</div></div>","PeriodicalId":256,"journal":{"name":"Bioorganic & Medicinal Chemistry Letters","volume":"121 ","pages":"Article 130161"},"PeriodicalIF":2.5,"publicationDate":"2025-03-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143584250","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Development of 9H-purine scaffold as novel CDK2 inhibitors: Design, synthesis, and biological evaluation","authors":"Yan Zhang ,&nbsp;Xiya Liu ,&nbsp;Ziming Li ,&nbsp;Xia Wang ,&nbsp;Chunlei Tang","doi":"10.1016/j.bmcl.2025.130166","DOIUrl":"10.1016/j.bmcl.2025.130166","url":null,"abstract":"<div><div>Cyclin-dependent kinase 2 (CDK2), a crucial regulator in multiple oncogenic signaling pathways, has emerged as a promising target for the development of innovative anticancer therapies and overcoming resistance to CDK4/6 inhibitors. In this study, three series of compounds were designed and synthesized, using the CDK2 inhibitor fadraciclib (CYC065) as the lead compound, with 9<em>H</em>-purine as the core structure. The design incorporated reported structure-activity relationship data and utilized computer-aided drug design techniques. Compounds in series <strong>1</strong> explored the binding mode between the ATP ribose binding site in CDK2 and C2 substituents, while compounds in series <strong>2</strong> and <strong>3</strong> validated the feasibility of modifying the specific binding region with different substituents and investigated the effects of filling the CDK2 hydrophobic pocket at the N9 position with alkyl substituents. Three compounds, <strong>1f</strong>, <strong>2e</strong>, and <strong>3a</strong>, demonstrated remarkable activity against CDK2-cyclin E2. Notably, <strong>3a</strong> exhibited the most potent effect, with a CDK2-cyclin E2 IC₅₀ value of 6.0 ± 0.1 nM, an MV4–11 IC₅₀ value of 489.2 ± 0.2 nM, and excellent selectivity for CDK2. This study evaluated the impact of substitutions at the 2, 6, and 9 positions of the purine ring on the activity of CDK2 small molecule inhibitors. The findings offer a theoretical foundation for future research, broadening the structural diversity and scope of CDK2 inhibitor studies.</div></div>","PeriodicalId":256,"journal":{"name":"Bioorganic & Medicinal Chemistry Letters","volume":"122 ","pages":"Article 130166"},"PeriodicalIF":2.5,"publicationDate":"2025-03-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143584252","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Discovery of Flavonol derivatives as porcine reproductive and respiratory syndrome virus inhibitors","authors":"Zhi-Zheng Wang ,&nbsp;Chen-Xu Xiao ,&nbsp;Wen-Li Huang ,&nbsp;Yang Hu ,&nbsp;Hui-Ting Zhang ,&nbsp;Zhang Liu ,&nbsp;Sheng-Hao Peng ,&nbsp;Zigong Wei","doi":"10.1016/j.bmcl.2025.130162","DOIUrl":"10.1016/j.bmcl.2025.130162","url":null,"abstract":"<div><div>Porcine reproductive and respiratory syndrome virus (PRRSV) causes serious threat to the global pig industry, and there was still no efficient treatment for porcine reproductive and respiratory syndrome (PRRS). Flavonol compounds were reported to show antiviral activity against a series of different virus. In this study, we designed a series of flavonol derivatives as promising lead structure for PRRSV inhibitors. A flavonol derivative database with diverse structures was first generated, and their anti-PRRSV activity were test. Among these compounds, compound <strong>4s</strong> showed promising anti-PRRSV activity with EC₅₀ values of 0.45 μM. In addition, it exhibited low cytotoxicity with CC₅₀ higher than 100 μM. We also found that compound <strong>4s</strong> inhibited PRRSV might be by repressing the activity of nsp4 protease. Molecular modeling study revealed that compound <strong>4s</strong> binding to nsp4 mainly relies on a salt bridge and hydrophobic interaction. Our results might provide a new way for the development of PRRSV inhibitors.</div></div>","PeriodicalId":256,"journal":{"name":"Bioorganic & Medicinal Chemistry Letters","volume":"121 ","pages":"Article 130162"},"PeriodicalIF":2.5,"publicationDate":"2025-03-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143584255","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"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 diphenyl ether-based kaiso inhibitors with enhanced potency","authors":"Taofeng Lin ,&nbsp;Zhongqi Li ,&nbsp;Juanchan Yuan ,&nbsp;Tinfeng Ren ,&nbsp;Wan Pang ,&nbsp;Songhui Xu","doi":"10.1016/j.bmcl.2025.130158","DOIUrl":"10.1016/j.bmcl.2025.130158","url":null,"abstract":"<div><div>Kaiso, a potential target for the treatment of lung cancer. Our research focuses on Kaiso inhibitros. Through virtual screening and molecular dynamic simulations, we discovered a promising Kaiso inhibitor called compound <strong>5</strong> (ZINC20577650). By modifying the structure of compound <strong>5</strong>, a series of novel Kaiso inhibitors that contain a diphenyl ether ring were synthesized. Among them, compound <strong>20</strong> exhibited the strongest inhibitory activity against A549 cells (IC₅₀ = 0.34 μM). Notably, its inhibitory activity surpassed that of the positive control <strong>MIRA-1</strong> (IC₅₀ = 654.065 μM). Molecular docking and dynamic studies revealed that the binding of the compound's amino and ester moieties to the active site of kaiso protein, as well as the extension of the benzene ring towards the Asn561 position in the cavity, contributed significantly to its potency. These findings provide valuable insights for the development of new Kaiso inhibitors.</div></div>","PeriodicalId":256,"journal":{"name":"Bioorganic & Medicinal Chemistry Letters","volume":"121 ","pages":"Article 130158"},"PeriodicalIF":2.5,"publicationDate":"2025-03-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143571741","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Synthesis, antiproliferative activity, and biological profiling of C-19 trityl and silyl ether andrographolide analogs in colon cancer and breast cancer cells","authors":"Tiffany Gu ,&nbsp;Rushika Raval ,&nbsp;Zachary Bashkin ,&nbsp;Carina Zhou ,&nbsp;Sanghyuk Ko ,&nbsp;Natalie Kong ,&nbsp;Seoyeon Hong ,&nbsp;Aditya Bhaskara ,&nbsp;Samarth Shah ,&nbsp;Aditi Joshi ,&nbsp;Samahith Thellakal ,&nbsp;Kaitlyn Rim ,&nbsp;Anushree Marimuthu ,&nbsp;Srishti Venkatesan ,&nbsp;Emma Wang ,&nbsp;Sophia Li ,&nbsp;Aditi Jayabalan ,&nbsp;Alice Tao ,&nbsp;Yilin Fang ,&nbsp;Lorelei Xia ,&nbsp;Edward Njoo","doi":"10.1016/j.bmcl.2025.130163","DOIUrl":"10.1016/j.bmcl.2025.130163","url":null,"abstract":"<div><div>Andrographolide, a labdane diterpenoid isolated from <em>Andrographis paniculata</em>, putatively functions through covalent inhibition of NF-κB, a transcription factor that modulates tumor survival and metastasis. Previous studies have found that functionalization of the C-19 hydroxyl alters the primary mode of action from inhibition of NF-κB to the modulation of the Wnt1/β-catenin signaling pathway. Here, we synthesized a series of twelve C-19 trityl and silyl ether analogs, including three novel substituted trityl analogs and four novel substituted silyl analogs of andrographolide. MTT assays revealed cell line selectivity between colorectal and breast cancer cells, which is consistent with known mechanisms of β-catenin-driven cell proliferation in colorectal cancer cell lines. Most compounds exhibited cell line specific antiproliferative activity in HCT-116 and HT-29 colorectal cancer cell lines. Specifically, within 24 h, C-19 analogs of andrographolide exhibit far more limited antiproliferative activity in MCF-7 breast cancer cells compared to HCT-116, HT-29, and MDA-MB-231 cells. Through <em>in vitro</em> TNF-α-dependent NF-κB reporter and Wnt1-dependent luciferase reporter assays, we observed that several analogs generally exhibit greater inhibitory activity compared to andrographolide. Fluorescence imaging demonstrated that cells treated with andrographolide and its C-19 analogs retained similar distributions of active β-catenin, but notable differences in antiproliferative potency upon co-delivery with GSK-3β inhibitor CHIR99021 indicate that several lead compounds exhibit attenuated biological activity selectively in HT-29 cells. Collectively, this work indicates that modest structural modifications at C-19 of andrographolide can have profound implications for its biological activity in mechanisms connected to its anticancer activity.</div></div>","PeriodicalId":256,"journal":{"name":"Bioorganic & Medicinal Chemistry Letters","volume":"121 ","pages":"Article 130163"},"PeriodicalIF":2.5,"publicationDate":"2025-03-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143562694","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Structure-activity of Bastadins from the marine sponge Ianthella basta. Modulators of the RYR1 Ca2+ channel","authors":"Melanie A. Franklin ,&nbsp;Mariam N. Salib ,&nbsp;Juliette Gafni ,&nbsp;Isaac N. Pessah ,&nbsp;Tadeusz F. Molinski","doi":"10.1016/j.bmcl.2025.130165","DOIUrl":"10.1016/j.bmcl.2025.130165","url":null,"abstract":"<div><div>The RYR1 Ca²⁺ channel mediates essential steps of excitation-contraction in skeletal muscle. Bastadins-5 and -6, highly brominated macrodilactams assembled from tyrosine and tyramine by the marine sponge <em>Ianthella basta</em>, were identified as potent sensitizers of RYR1 channel activation. Here, we present a structure-activity relationships study of a wide panel of bastadins, and related analogs, and define the minimum requirements for stabilizing the RYR1 complex open or closed conformations.</div></div>","PeriodicalId":256,"journal":{"name":"Bioorganic & Medicinal Chemistry Letters","volume":"121 ","pages":"Article 130165"},"PeriodicalIF":2.5,"publicationDate":"2025-03-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143562693","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Phenyl urea based adjuvants for β-lactam antibiotics against methicillin resistant Staphylococcus aureus","authors":"Hailey S. Butman ,&nbsp;Monica A. Stefaniak ,&nbsp;Danica J. Walsh ,&nbsp;Vijay S. Gondil ,&nbsp;Mikaeel Young ,&nbsp;Andrew H. Crow ,&nbsp;Ansley M. Nemeth ,&nbsp;Roberta J. Melander ,&nbsp;Paul M. Dunman ,&nbsp;Christian Melander","doi":"10.1016/j.bmcl.2025.130164","DOIUrl":"10.1016/j.bmcl.2025.130164","url":null,"abstract":"<div><div>Penicillin binding protein 4 (PBP4) is essential for <em>Staphylococcus aureus</em> cortical bone osteocyte lacuno-canalicular network (OLCN) invasion, which causes osteomyelitis and serves as a bacterial niche for recurring bone infection. Moreover, PBP4 is also a key determinant of <em>S. aureus</em> resistance to fifth-generation cephalosporins (ceftobiprole and ceftaroline). From these perspectives, the development of <em>S. aureus</em> PBP4 inhibitors may represent dual functional therapeutics that prevent osteomyelitis, and reverse PBP4-mediated β-lactam resistance. A high-throughput screen for small molecules that inhibit <em>S. aureus</em> PBP4 function identified compound <strong>1</strong>. We recently described a preliminary structure activity relationship (SAR) study on <strong>1</strong>, identifying several compounds with increased PBP4 inhibitory activity, some of which also inhibit PBP2a. Herein, we expand our exploration of phenyl ureas as antibiotic adjuvants, investigating their activity with penicillins and additional cephalosporins against PBP2a-mediated methicillin-resistant <em>S. aureus</em> (MRSA). We screened the previously reported pilot library, and prepared an additional series of phenyl ureas based on compound <strong>1</strong>. Lead compounds potentiate multiple β-lactam antibiotics, lowering minimum inhibitory concentrations (MICs) below susceptibility breakpoints, with up to 64-fold reductions in MIC.</div></div>","PeriodicalId":256,"journal":{"name":"Bioorganic & Medicinal Chemistry Letters","volume":"121 ","pages":"Article 130164"},"PeriodicalIF":2.5,"publicationDate":"2025-03-03","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143565733","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Bulky substrates of isoleucine 2-epimerase: α-Neopentylglycine and NV-5138","authors":"Noa T. Sorbara ,&nbsp;Amanda K.A. Black ,&nbsp;Stephen L. Bearne","doi":"10.1016/j.bmcl.2025.130160","DOIUrl":"10.1016/j.bmcl.2025.130160","url":null,"abstract":"<div><div>Isoleucine 2-epimerase from <em>Lactobacillus buchneri</em> (<em>Lb</em>IleE) catalyzes the pyridoxal 5′-phosphate-dependent, reversible, racemization or epimerization of nonpolar amino acids at the C-2 position. The integral role of the enzyme in the biosynthesis of branched-chain <span>d</span>-amino acids makes it a potential target for the development of antimicrobial agents. Probing the hydrophobic active-site pocket with a series of alkyl boronic acids, we show that the hydrophobic pocket accommodates the neopentyl group with enhanced binding affinity relative to the sec-butyl group. Subsequently, we show that <em>Lb</em>IleE catalyzes the racemization of <span>l</span>- and <span>d</span>-α-neopentylglycine, exhibiting binding affinities for these substrates 6- and 24-fold greater than those for <span>l</span>-Ile and <span>d</span>-<em>allo</em>-Ile, but with catalytic efficiencies (<em>k</em>_cat/<em>K</em>_m) reduced 46- and 27-fold, respectively. NV-5138 is a ligand of the leucine-binding site of Sestrin2, which activates the mechanistic target of rapamycin complex1 (mTORC1) and is structurally similar to α-neopentylglycine. Our demonstration that <em>Lb</em>IleE catalyzes the racemization of <span>l</span>-NV-5138 (<em>k</em>_cat/<em>K</em>_m = 2.2 ± 0.2 s⁻¹ mM⁻¹), along with the fact that <em>L</em>. <em>buchneri</em> can be present in the human gut microbiome, suggests that formation of <span>d</span>-NV-5138 could occur in humans when <span>l</span>-NV-5138 is used as a pharmacological intervention for depression.</div></div>","PeriodicalId":256,"journal":{"name":"Bioorganic & Medicinal Chemistry Letters","volume":"122 ","pages":"Article 130160"},"PeriodicalIF":2.5,"publicationDate":"2025-03-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143555511","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Discovery of 1,3-Disubstituted Pyrazole derivatives as Mycobacterium tuberculosis inhibitors","authors":"Guoquan Wan ,&nbsp;Chao Gao ,&nbsp;Xiaorui Zhang ,&nbsp;Huapei Qiu ,&nbsp;Qifan Tang ,&nbsp;Jumei Zeng ,&nbsp;Luoting Yu","doi":"10.1016/j.bmcl.2025.130156","DOIUrl":"10.1016/j.bmcl.2025.130156","url":null,"abstract":"<div><div>Tuberculosis is a global epidemic caused by <em>Mycobacterium tuberculosis</em>, predominantly impacting underprivileged regions worldwide. Here, we identified a novel 1,3-disubstituted pyrazole derivative, compound <strong>A</strong>, that exhibits antitubercular activity through <em>in vitro</em> screening. Further SAR studies resulted in the identification of compounds <strong>4c</strong> and <strong>6b</strong>, which exhibited improved antitubercular activity, with MIC values of 5.34 and 5.04 μg/mL against H37Ra, respectively. Additionally, compounds <strong>4c</strong> and <strong>6b</strong> exhibited favorable safety profiles, showing no obvious toxicity to Vero, A549, and HepG2 cell lines. Our docking studies suggest that PptT may serve as one of the potential targets for these compounds. These encouraging results provide valuable insights for the development of novel structured antitubercular agents.</div></div>","PeriodicalId":256,"journal":{"name":"Bioorganic & Medicinal Chemistry Letters","volume":"121 ","pages":"Article 130156"},"PeriodicalIF":2.5,"publicationDate":"2025-02-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143536228","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Synthesis and evaluation of a targeted PET radioligand [18F]FCOB02 for monoamine oxidase B","authors":"Zhixiong Zhang ,&nbsp;Ge Zhang ,&nbsp;Jingquan Xue ,&nbsp;Yuxuan Zhang ,&nbsp;Yu Liu ,&nbsp;Wenjiang Yang ,&nbsp;Jianjun Wang","doi":"10.1016/j.bmcl.2025.130157","DOIUrl":"10.1016/j.bmcl.2025.130157","url":null,"abstract":"<div><div>Monoamine oxidase B (MAO-B) is a membrane-bound flavinase that plays an important role in the regulation of monoamine neurotransmission. Positron emission tomography (PET) provides a way to study the molecular mechanisms of MAO-B-related diseases and to evaluate the effects of drugs. In this study, we designed and synthesized [¹⁸F]FCOB02, a 4-methylcoumarin-like targeting probe.[¹⁸F]FCOB02 is straightforward to synthesize and has a high affinity for MAO-B with an IC₅₀ = 10.68 ± 3.25 nM. Successful radiolabeling with fluorine-18 was achieved, resulting in a labeling rate of 35 % along with favorable lipid solubility (log <em>D</em>_7.4 = 2.4). Automated radiolabelling was achieved after optimization of the conditions. The radiochemical yield was 9.6 % ± 1.2 %(<em>n</em> = 3) with good radiochemical purity (&gt;98 %), good stability in saline for 4 h and high specific activity (105.08 ± 19GBq/μmol，n = 3). Biodistribution studies conducted in mice revealed significant initial brain uptake of 8.22 ± 0.86 % ID/g at 2 min post-injection, followed by rapid metabolism primarily via the liver and kidneys. Brain uptake was comparable to the same type of probe [¹⁸F]SMBT-1 (brain _2min = 7.85 % ID/g). PET-CT images of [¹⁸F]FCOB02 in SD rats showed significant differences in brain uptake before and after inhibition by the inhibitor L-deprenyl. Whole brain uptake was reduced by 20 % after inhibition, indicating specific uptake of the probe in the brain, with a 40-min brain clearance rate of 81 %. The potential utility of [¹⁸F]FCOB02 for achieving specific MAO-B imaging as well as quantitative analysis in vivo warrants further investigation regarding its clinical translational value.</div></div>","PeriodicalId":256,"journal":{"name":"Bioorganic & Medicinal Chemistry Letters","volume":"121 ","pages":"Article 130157"},"PeriodicalIF":2.5,"publicationDate":"2025-02-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143512106","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}