European Journal of Medicinal Chemistry最新文献

{"title":"Discovery of piperazine-based multi-site occupying coronavirus M^pro inhibitors with potent and broad-spectrum antiviral activity.","authors":"Bing Ye, Myoung Kyu Lee, Letian Song, Yeon Seo Jeon, Mei Wang, Xianghan Bai, Shenghua Gao, Meehyein Kim, Peng Zhan, Xinyong Liu","doi":"10.1016/j.ejmech.2026.119248","DOIUrl":"https://doi.org/10.1016/j.ejmech.2026.119248","url":null,"abstract":"<p><p>The continuous evolution of SARS-CoV-2 and the emergence of drug-resistant variants underscore the urgent need for broad-spectrum antiviral agents targeting conserved viral proteins. The main protease (M^pro) represents a promising target due to its essential role in coronavirus replication. In this study, we report the discovery and optimization of a novel series of piperazine-based M^pro inhibitors using a multi-site binding strategy guided by analysis of conserved residues within the coronavirus M^pro active sites. Starting from the noncovalent lead GC-14, systematic optimization of substituents occupying the S1', S1, S2, and S4 subsites of M^pro led to the development of the noncovalent inhibitor GY-e2, which showed improved inhibitory efficacy against both SARS-CoV-2 and SARS-CoV M^pro. To further enhance its antiviral efficacy in cellular models, reactive warheads targeting C145 were incorporated into the scaffold to generate covalent inhibitors. This strategy yielded the isomeric compounds Y-U0-R and Y-U0-S, which displayed potent M^pro inhibition and markedly enhanced antiviral activity in SARS-CoV-2-infected Calu-3 cells. Moreover, both compounds exhibited broad-spectrum antiviral activity against other human coronaviruses, and notably remained effective against the two major Nirmatrelvir-resistant strains evaluated in this study. Mechanistic studies further confirmed kinetically stable binding and time-dependent inhibition of Y-U0-R, supporting the rationale of covalent inhibitor design. These findings highlight the utility of structure-based design for the development of promising broad-spectrum anti-coronavirus agents.</p>","PeriodicalId":314,"journal":{"name":"European Journal of Medicinal Chemistry","volume":"319 ","pages":"119248"},"PeriodicalIF":6.7,"publicationDate":"2026-08-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148872517","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 “Machine learning-guided discovery of covalent sortase A inhibitors targeting MRSA virulence” [Eur. J. Med. Chem. (2026) 318, 119139]","authors":"Xu-liang Xu, Ti-ti Ying, Xiao-wen Wu, Yun-jun Chen, Gang-ao Hu, Yu-tian Guan, Shi-yi Liu, He Wang, Mohamed Seif, Mahmoud Emam, Hong Wang, Wei Hou, Bin Wei","doi":"10.1016/j.ejmech.2026.119230","DOIUrl":"https://doi.org/10.1016/j.ejmech.2026.119230","url":null,"abstract":"","PeriodicalId":314,"journal":{"name":"European Journal of Medicinal Chemistry","volume":"70 1","pages":"119230"},"PeriodicalIF":6.7,"publicationDate":"2026-08-18","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148756606","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":"Carbohydrate and heterocycle-based β-Glucocerebrosidase Inhibitors: State-of-art and Emerging Relationship with Cancer Treatment","authors":"Francesca Milano, Francesca Clemente, Francesca Cardona, Andrea Goti, Alessandra Quarta, Marco Marradi, Andrea Ragusa, Camilla Matassini","doi":"10.1016/j.ejmech.2026.119254","DOIUrl":"https://doi.org/10.1016/j.ejmech.2026.119254","url":null,"abstract":"","PeriodicalId":314,"journal":{"name":"European Journal of Medicinal Chemistry","volume":"4 2 1","pages":"119254"},"PeriodicalIF":6.7,"publicationDate":"2026-08-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148756608","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":"Bridging DNA Damage and cGAS-STING Activation: Platinum (IV) Prodrugs as Single-Molecule Chemo-Immunotherapeutics","authors":"Junkang Ren, Jiani Wu, Xinyu Dai, Feihong Chen","doi":"10.1016/j.ejmech.2026.119210","DOIUrl":"https://doi.org/10.1016/j.ejmech.2026.119210","url":null,"abstract":"","PeriodicalId":314,"journal":{"name":"European Journal of Medicinal Chemistry","volume":"56 1","pages":""},"PeriodicalIF":6.7,"publicationDate":"2026-08-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148716734","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":"CADD-Based Discovery of Novel Heterocyclic Pyrimidine-Based CDK4/6 Inhibitors: Design, Synthesis, and Anti-Breast Cancer Activity Studies","authors":"Xinya Lv ,&nbsp;Xiaoling Huang ,&nbsp;Lulu Tian ,&nbsp;Shidi Xu ,&nbsp;Yujie Zhan ,&nbsp;Hanrui Hou ,&nbsp;Dajun Zhang ,&nbsp;Linxiao Wang ,&nbsp;Shan Xu","doi":"10.1016/j.ejmech.2026.118932","DOIUrl":"10.1016/j.ejmech.2026.118932","url":null,"abstract":"&lt;div&gt;&lt;ul&gt;&lt;li&gt;&lt;span&gt;•&lt;/span&gt;&lt;span&gt;&lt;div&gt;Forty novel heterocyclic pyrimidine compounds were designed, screened, and synthesized using a CADD strategy as highly potent CDK4/6 inhibitors.&lt;/div&gt;&lt;/span&gt;&lt;/li&gt;&lt;li&gt;&lt;span&gt;•&lt;/span&gt;&lt;span&gt;&lt;div&gt;The lead compound 3c exhibits potent CDK4/6 kinase inhibitory activity, with an IC50 in the nM range.&lt;/div&gt;&lt;/span&gt;&lt;/li&gt;&lt;li&gt;&lt;span&gt;•&lt;/span&gt;&lt;span&gt;&lt;div&gt;Compound 3c induces G1 phase arrest and apoptosis in MCF-7 cancer cells by inhibiting the phosphorylation of the Rb protein.&lt;/div&gt;&lt;/span&gt;&lt;/li&gt;&lt;li&gt;&lt;span&gt;•&lt;/span&gt;&lt;span&gt;&lt;div&gt;The lead compound demonstrates good in vivo tumor-suppressing activity and acceptable biosafety, making it worthy of further development.&lt;/div&gt;&lt;/span&gt;&lt;/li&gt;&lt;/ul&gt;&lt;/div&gt;&lt;div&gt;&lt;div&gt;Cyclin-dependent kinase 4/6 (CDK4/6) plays a pivotal role in cell cycle regulation, and its abnormal activation is closely associated with the initiation and progression of breast cancer.1 However, the limited number of clinically available CDK4/6 inhibitors restricts treatment options. This study focuses on the design, synthesis, and antitumor activity investigation of novel CDK4/6 inhibitors.Employing computer-aided drug design (CADD) strategies and utilizing drug-like and bioisostere principles, we innovatively introduced pyridine-2-aminopyrimidine, thieno[3,2-d]pyrimidine, and pyrazolo[1,5-a]pyrimidine as core skeletal structures to design and screen 250 compound molecules. Based on computational results, including molecular docking and MM/GBSA binding free energy, 40 potential novel CDK4/6 inhibitors were selected for synthesis.Cellular assays validated that compound 3c exhibited the strongest inhibitory activity against CDK4/6 in breast cancer cell lines, with IC&lt;sub&gt;50&lt;/sub&gt; values of 0.11 ± 0.01 μM (MCF-7), 0.21 ± 0.01 μM (4T1), and 0.12 ± 0.01 μM (MDA-MB-231). And compound &lt;strong&gt;3c&lt;/strong&gt; demonstrated favorable CDK4/6 inhibition rates and showed a certain degree of selectivity among 23 kinases. In vitro mechanistic studies revealed that &lt;strong&gt;3c&lt;/strong&gt; consistently inhibited cell colony formation and migration. Furthermore, &lt;strong&gt;3c&lt;/strong&gt; effectively arrested the MCF-7 cell cycle at the G1 phase and induced apoptosis. In the MCF-7 xenograft model, compound &lt;strong&gt;3c&lt;/strong&gt; achieved a tumor inhibition rate of 45.20%, highlighting its significant potential as a therapeutic CDK4/6 inhibitor.&lt;/div&gt;&lt;/div&gt;&lt;div&gt;Cyclin-dependent kinase 4/6 (CDK4/6) plays a pivotal role in cell cycle regulation, and its abnormal activation is closely associated with the initiation and progression of breast cancer.1 However, the limited number of clinically available CDK4/6 inhibitors restricts treatment options. This study focuses on the design, synthesis, and antitumor activity investigation of novel CDK4/6 inhibitors.Employing computer-aided drug design (CADD) strategies and utilizing drug-like and bioisostere principles, we innovatively introduced pyridine-2-aminopyrimidine, thieno[3,2-d]pyrimidine, and pyrazolo[1,5-a]pyrimidine as co","PeriodicalId":314,"journal":{"name":"European Journal of Medicinal Chemistry","volume":"315 ","pages":"Article 118932"},"PeriodicalIF":5.9,"publicationDate":"2026-05-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"147999287","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 novel ENPP1 inhibitors with benzotriazole core for cancer immunotherapy","authors":"Junghwan Choi ,&nbsp;Sunwoo Lee ,&nbsp;Yong-Yea Park ,&nbsp;Jihun Kim ,&nbsp;Haein Kim ,&nbsp;Kyeongwon Moon ,&nbsp;Sunyoung Park ,&nbsp;Eun Kyung Yoo ,&nbsp;Chang Won Min ,&nbsp;Hyouk Woo Lee ,&nbsp;Hyun-Ju Park ,&nbsp;Pargat Singh ,&nbsp;Sungjoon Kim ,&nbsp;Chan Sun Park ,&nbsp;In Su Kim","doi":"10.1016/j.ejmech.2026.118666","DOIUrl":"10.1016/j.ejmech.2026.118666","url":null,"abstract":"<div><div>The cGAS-STING signaling pathway is an essential mechanism in the recruitment and activation of innate and adaptive immune cells to exert an antitumor response in cancer immunotherapy. cGAMP is a crucial immunotransmitter, which is potentially degraded by ENPP1, resulting in the deactivation of STING-mediated antitumor immune responses. We herein describe the design, synthesis, and biological evaluation of novel ENPP1 inhibitors containing a benzotriazole core and a sulfonimidamide Zn binder. Notably, compound <strong>44a</strong> demonstrated potent and selective ENPP1 inhibition with an IC₅₀ value of 13.1 nM and effectively activated the STING pathway in HCT116-Dual™ cells. Additionally, compound <strong>44a</strong> exhibited a notable release of cytokines in THP-1 cell lines, thereby enhancing the innate immune response. The oral administration of compound <strong>44a</strong> displayed remarkable antitumor efficacy in the MC38 syngeneic mouse model without notable toxicity. Therefore, compound <strong>44a</strong> can be considered a promising candidate as a selective and orally bioavailable ENPP1 inhibitor.</div></div>","PeriodicalId":314,"journal":{"name":"European Journal of Medicinal Chemistry","volume":"307 ","pages":"Article 118666"},"PeriodicalIF":5.9,"publicationDate":"2026-04-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146153257","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":"Xanthine oxidase inhibitors for gout: Applications and novel drug development","authors":"Weiping Lyu ,&nbsp;Haoming Qin ,&nbsp;Xiaonan Zhou ,&nbsp;Yihan Zhang ,&nbsp;Dehua Lu ,&nbsp;Yongxiang Shao ,&nbsp;Yanming Chen ,&nbsp;Mingxiu Liang ,&nbsp;Qi Li ,&nbsp;Xiaowei Chi ,&nbsp;Liangren Zhang ,&nbsp;Cheng Shi ,&nbsp;Zhenming Liu","doi":"10.1016/j.ejmech.2026.118619","DOIUrl":"10.1016/j.ejmech.2026.118619","url":null,"abstract":"<div><div>Hyperuricemia is a well-established direct trigger of gouty arthritis. Xanthine oxidase (XO), the rate-limiting enzyme in uric acid production, represents a core therapeutic target for gout. Although XO inhibitors like allopurinol and febuxostat are widely-used clinically, their limitations, including severe hypersensitivity and cardiovascular risks, necessitate the continuous pursuit of safer and more efficient agents. This review provides a systematic and critical assessment of recent advances in XO inhibitor research, proposing for the first time a unified classification framework based on the evolution of drug design strategies. We comprehensively cover diverse chemical entities, from structure-based, rationally designed compounds to natural products and their corresponding analogs, with a particular emphasis on cutting-edge strategies designed to overcome existing drawbacks. These include dual-target inhibitors (e.g., targeting XO/URAT1 or XO/NLRP3) and drug repurposing. By delving into the structure-activity relationships within each inhibitor class, we identify crucial pharmacophores and optimization principles. Finally, the review offers a forward-looking perspective, critically discussing current research challenges and outlining future directions, such as leveraging artificial intelligence and advanced computational simulations for lead optimization. This work is intended to serve as a clear theoretical blueprint and a practical source of inspiration for medicinal chemists designing the next generation of highly effective and low-toxicity anti-gout therapeutics.</div></div>","PeriodicalId":314,"journal":{"name":"European Journal of Medicinal Chemistry","volume":"307 ","pages":"Article 118619"},"PeriodicalIF":5.9,"publicationDate":"2026-04-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146135339","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":"Structural optimization of AR and AR-V7 degraders incorporating silicon-based hydrophobic tags for treatment of castration-resistant prostate cancer","authors":"Lei Xu ,&nbsp;Mengmeng Wang ,&nbsp;Yanshuo Cheng ,&nbsp;Hanhan Kuang ,&nbsp;Yijing Zhu ,&nbsp;Ning Liu ,&nbsp;Qianqian Wang ,&nbsp;Shicong Li ,&nbsp;Jiefu Wang ,&nbsp;Junfeng Wang ,&nbsp;Ziqi Huang ,&nbsp;Ranlu Liu ,&nbsp;Shuangwei Liu ,&nbsp;Kun Zhang ,&nbsp;Guang Yang","doi":"10.1016/j.ejmech.2026.118617","DOIUrl":"10.1016/j.ejmech.2026.118617","url":null,"abstract":"<div><div>Androgen receptor splice variant 7 (AR-V7) plays a crucial role in the malignant progression of castration-resistant prostate cancer (CRPC). Current research has demonstrated that the development of novel AR-V7 degraders holds broad prospects and is expected to serve as a clinical therapeutic regimen for this disease. In the present work, we utilized structural analogs of enzalutamide to conjugate a silicon-containing hydrophobic tag (SiHyT) moiety via Click chemistry, achieving the selective degradation of the androgen receptor (AR) and AR-V7. Mechanistic studies revealed that the degrader disrupted the interactions between AR/AR-V7 and HSP90. This disruption further prompted the E3 ubiquitin ligase helicase-like transcription factor (HLTF) to recognize AR and AR-V7, followed by their ubiquitination and degradation in CRPC cell lines. Additionally, the active compound exhibited favorable pharmacokinetic properties and metabolic profiles. In both <em>in vitro</em> and <em>in vivo</em> experiments, this degrader displayed more potent activity than enzalutamide in inhibiting the proliferation and migration of CRPC cells. This study expands the application scope of the silicon-containing hydrophobic tag (SiHyT) strategy and provides an alternative design concept for the development of drugs targeting the degradation of AR/AR-V7 in the treatment of CRPC.</div></div>","PeriodicalId":314,"journal":{"name":"European Journal of Medicinal Chemistry","volume":"307 ","pages":"Article 118617"},"PeriodicalIF":5.9,"publicationDate":"2026-04-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146095637","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":"New antitubercular pretomanid analogues as potent payloads in polymeric micelles: Leveraging zebrafish assays to accelerate lead optimisation","authors":"Andrew M. Thompson ,&nbsp;Nils-Jørgen K. Dal ,&nbsp;Francesca Boldrin ,&nbsp;Noelia Alonso-Rodriguez ,&nbsp;Gabriela Schäfer ,&nbsp;Kerstin Johann ,&nbsp;Martin Speth ,&nbsp;Laura Cioetto-Mazzabò ,&nbsp;Adrián Pál ,&nbsp;Jana Korduláková ,&nbsp;Matthias Barz ,&nbsp;Federico Fenaroli ,&nbsp;William A. Denny ,&nbsp;Gareth Griffiths","doi":"10.1016/j.ejmech.2026.118622","DOIUrl":"10.1016/j.ejmech.2026.118622","url":null,"abstract":"<div><div>Third-generation derivatives of the tuberculosis drug pretomanid featuring acetylene-bridged aryl-heteroaryl or heterotriaryl side chains were designed as novel agents for nanoparticle-based delivery, seeking better efficacy and safety. While all nitro compounds retained excellent activity against <em>Mycobacterium tuberculosis</em>, several examples in the latter class excelled as having potency superior to the original lead (<strong>7</strong>) but equivalent to or reduced lipophilicity, implying enhanced lipophilic efficiency. Initial studies suggested a similar mode of action against the related fish pathogen, <em>M. marinum</em>; therefore, fourteen candidates were further assessed as micellar formulations in <em>M. marinum-</em>infected zebrafish embryo assays. Overall, the best new analogue was <strong>14</strong> (the 6-amino-linked congener of <strong>7</strong>), which was non-toxic and displayed efficacy comparable to <strong>7</strong> in both the blood and neural tube <em>M. marinum</em> infection models. Lead <strong>14</strong> also exhibited high microsomal stability, moderate cell permeability in an MDR1-MDCKII screen, and an enhanced pharmacokinetic profile in mice, with 93 % oral bioavailability.</div></div>","PeriodicalId":314,"journal":{"name":"European Journal of Medicinal Chemistry","volume":"307 ","pages":"Article 118622"},"PeriodicalIF":5.9,"publicationDate":"2026-04-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146089516","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":"Advances in pyrimidine-like heterocyclic scaffolds: Innovative synthetic method for malic enzyme inhibition in pancreatic ductal adenocarcinoma (PDAC) - A comprehensive review","authors":"Shubham Mehta ,&nbsp;Iti Patel ,&nbsp;Gautam Patel","doi":"10.1016/j.ejmech.2026.118657","DOIUrl":"10.1016/j.ejmech.2026.118657","url":null,"abstract":"<div><div>Pancreatic cancer remains one of the most lethal cancers of the 21st century due to extensive metabolic reprogramming and a highly adaptable tumor microenvironment that fosters relentless growth and resistance to treatment. Molecular docking studies targeted on malic enzyme facilitate the discovery of possible inhibitors that interfere with pancreatic cancer metabolism. Understanding the molecular circuitry of this disease, especially through the use of heterocyclic frameworks that inhibit metabolic needs specific to cancer, has enabled targeted therapy. Pyrimidine and fused-pyrimidine structures have become unique scaffolds because they are very good at breaking down metabolic checkpoints that are important for tumors to stay alive. Pyrimidine derivatives are at the forefront of developing next-generation anticancer drugs because they inhibit the malic enzyme (ME), which is a key regulator of redox homeostasis and biosynthetic flux in pancreatic cancers. This review gives a full picture of the synthetic methods that make it easy to quickly change the structure of pyrimidine-based pharmacophores. Some of these strategies are old, like Vorbrüggen glycosylation and HATU-mediated peptide coupling. Others are new, like chalcone-guanidine cyclocondensation and modular multi-component protocols. Pyrimidine scaffolds are crucial elements of precision oncology, evidenced by data from preclinical and clinical studies that underscore the therapeutic translatability of targeting metabolic abnormalities in pancreatic cancer. Even though chemotherapy, targeted therapy, and immunotherapy have all become better in the last few years, treating pancreatic cancer is still challenging due to its late diagnosis, the drug resistance, and the fact that there aren't many suitable options for treatment. Apart from that, there are still some big problems to solve, like metabolic redundancy, isoform-selective ME inhibition, and the tumor microenvironment, which makes treatment harder. To overcome these challenges, the amalgamation of multi-pathway inhibition, AI-driven lead optimization, and nanotechnology-facilitated targeted delivery offers considerable promise. This review emphasizes the crucial function of pyrimidine scaffolds in revolutionizing the therapeutic strategy for pancreatic cancer, linking mechanistic understanding to practical drug discovery.</div></div>","PeriodicalId":314,"journal":{"name":"European Journal of Medicinal Chemistry","volume":"307 ","pages":"Article 118657"},"PeriodicalIF":5.9,"publicationDate":"2026-04-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"146135332","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}