European Journal of Medicinal Chemistry Reports最新文献

{"title":"P-glycoprotein-independent cytotoxic effects of 5-aminopyrazole in L1210 leukemia cells","authors":"Lucia Sofrankova ,&nbsp;Jana Spaldova ,&nbsp;Pavol Stefik ,&nbsp;Branislav Pavilek ,&nbsp;Dusan Bortnak ,&nbsp;Lucia Pavlikova ,&nbsp;Ivana Zidekova ,&nbsp;Daniel Vegh ,&nbsp;Viktor Milata ,&nbsp;Albert Breier ,&nbsp;Zdena Sulova","doi":"10.1016/j.ejmcr.2025.100246","DOIUrl":"10.1016/j.ejmcr.2025.100246","url":null,"abstract":"<div><div>We previously investigated the cytotoxic effects of 5-aminopyrazoles (5-APs) on leukemia cells both negative and positive for P-glycoprotein (P-gp) expression, a common contributor to multidrug resistance. Five derivatives (A1-A5), each containing perfluorinated methylbenzene at the N3 nitrogen of the pyrazole ring, were tested on murine lymphoblastic cell line variants: parental S cells (P-gp positive), R cells (vincristine-resistant and P-gp positive), and T cells (human P-gp transfected). Among these, A1 and A4 exhibited the strongest effects, especially in R cells, with lesser but similar effects observed in S and T cells. Cell death assays revealed both apoptosis and necrosis, with apoptosis confirmed by DNA fragmentation and activation of caspases 3/7, 8, and, to a lesser extent, 9, suggesting a predominance of extrinsic apoptosis. The compounds also induced autophagy, identified by LysoTracker Green and monodansylcadaverine staining. All derivatives, except A5, suppressed P-gp activity, though they did not alter P-gp expression at the mRNA or protein level. Cell cycle analysis showed changes in the G0/G1 and S phases. The heightened sensitivity of R cells to 5-AP, despite P-gp expression, likely results from an altered phenotype due to vincristine-induced stress rather than from P-gp inhibition alone. This conclusion is supported by the fact that T cells expressing P-gp are as sensitive to 5-APs as S cells.</div></div>","PeriodicalId":12015,"journal":{"name":"European Journal of Medicinal Chemistry Reports","volume":"13 ","pages":"Article 100246"},"PeriodicalIF":0.0,"publicationDate":"2025-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143160278","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Corrigendum to: Advancements, challenges, and future frontiers in covalent inhibitors and covalent drugs: A review [Eur. J. Med. Chem. Rep. 5]","authors":"Muhammad Salman Hameed ,&nbsp;Hongxuan Cao ,&nbsp;Li Guo ,&nbsp;Lei Zeng ,&nbsp;Yanliang Ren","doi":"10.1016/j.ejmcr.2025.100254","DOIUrl":"10.1016/j.ejmcr.2025.100254","url":null,"abstract":"","PeriodicalId":12015,"journal":{"name":"European Journal of Medicinal Chemistry Reports","volume":"13 ","pages":"Article 100254"},"PeriodicalIF":0.0,"publicationDate":"2025-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143600502","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"New heterocyclic A1/A3 adenosine receptor ligands through molecular simplification strategies","authors":"Letizia Crocetti ,&nbsp;Abigail Pearce ,&nbsp;Venkat S. Vege ,&nbsp;Qi Xu ,&nbsp;Jing Xu ,&nbsp;Hannes Buthmann ,&nbsp;Maria Paola Giovannoni ,&nbsp;Gabriella Guerrini ,&nbsp;Francesca Catarzi ,&nbsp;Silvia Selleri ,&nbsp;Xianglin Huang ,&nbsp;Aneesh Chandran ,&nbsp;Graham Ladds ,&nbsp;Agostino Cilibrizzi","doi":"10.1016/j.ejmcr.2025.100253","DOIUrl":"10.1016/j.ejmcr.2025.100253","url":null,"abstract":"<div><div>In this paper we report the synthesis of new A₁/A₃ adenosine receptor antagonists designed as simplification products of the A₁ antagonists with pyrazolo[1′,5′:1,6]pyrimido [4,5-d]pyridazin-4(3H)-one scaffold previously developed by us. Notably, selective A₁R antagonists are promising therapeutic agents in Alzheimer's disease and for the treatment of cognitive deficits, while A₃R antagonists are potentially useful in the treatment of ischemia and certain types of cancer. Initial screening with NanoBRET competition binding assay revealed a number of products with pKi ≥5 for A₁R and A₃R. For some representative compounds the antagonist profiles, as well as their selectivity versus A_2AR and A_2BR, have been also validated by antagonizing NECA in cAMP accumulation. The most interesting compounds resulted the A₁/A₃ mixed antagonist <strong>3b</strong> (pKi = 6.41 and 6.29 for A₁R and A₃R respectively, pKb = 5.00 and 5.27 for the A_2aR and A_2bR) and the selective A₃R antagonist <strong>5c</strong> (pKi = 6.40, pKb values of 4.44, 6.17, 4.16, and 4.78 for the A₁R, A₃R, A_2aR and A_2bR, respectively). Furthermore, <em>in silico</em> simulations were carried out to study the molecular mechanism of the high affinity of <strong>3b</strong> for A₁/A₃Rs as well as the selectivity of <strong>5c</strong> for A₃R over A₁R. Overall, this work highlights new series of bicyclic small-molecules as valid candidates for further structural optimization towards the development of therapeutically relevant A₁/A₃ adenosine receptor antagonists.</div></div>","PeriodicalId":12015,"journal":{"name":"European Journal of Medicinal Chemistry Reports","volume":"13 ","pages":"Article 100253"},"PeriodicalIF":0.0,"publicationDate":"2025-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143454594","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Design, synthesis and evaluation of quinazoline-chalcone hybrids as inducers of cell-cycle arrest and apoptosis in breast cancer via DNA damage and CDK2/ATR inhibition","authors":"Giulia Rodrigues Stringhetta ,&nbsp;Eduardo Bustos Mass ,&nbsp;Izabela Natalia Faria Gomes ,&nbsp;Maria Clara Fonseca Peixoto ,&nbsp;Amanda Helena Tejada ,&nbsp;Luciane Susucchi ,&nbsp;Aryel José Alves Bezerra ,&nbsp;Pedro Victor Silva Resende ,&nbsp;Vinicius Vendrúsculo ,&nbsp;Rui Manuel Reis ,&nbsp;Dennis Russowsky ,&nbsp;Renato José Da Silva Oliveira","doi":"10.1016/j.ejmcr.2025.100250","DOIUrl":"10.1016/j.ejmcr.2025.100250","url":null,"abstract":"<div><div>In this study, a series of novel hybrid compounds, 2-arylquinazolinechalcones, were synthesized and their antitumoral activities were evaluated. Among them, compounds <strong>7b</strong> and <strong>7n</strong> exhibited the highest cytotoxicity and selectivity rates for the triple-negative breast cancer cell line MDA-MB-231. In 3D spheroid culture, <strong>7b</strong> and <strong>7n</strong> decreased viability and increased cell death. Both compounds induced cell death primarily through the extrinsic pathway and promoted cell cycle arrest in G0/G1, possibly through increased expression of p27 and subsequent reduction in CDK2 levels. Additionally, they may trigger oxidative stress and DNA damage, as evidenced by elevated levels of H2AX activation, and compromise DNA repair pathways mediated by ATR and CHK1. To further explore the mechanism behind the observed cell cycle arrest, we performed phospho-RTK and phospho-MAPK Reverse Phase Protein Arrays to investigate changes in the expression of activated RTKs and MAPKs after treatment with <strong>7b</strong> and <strong>7n</strong>, compared to the negative control. These findings suggest that <strong>7b</strong> and <strong>7n</strong> are promising candidates for further development as targeted therapies for triple-negative breast cancer.</div></div>","PeriodicalId":12015,"journal":{"name":"European Journal of Medicinal Chemistry Reports","volume":"13 ","pages":"Article 100250"},"PeriodicalIF":0.0,"publicationDate":"2025-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143420481","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Design, synthesis, and biological evaluation of substituted benzyl-triazolopyridine derivatives as non-hydroxamate based HDAC8 inhibitors","authors":"N.V.M. Rao Bandaru ,&nbsp;Ashna Fathima ,&nbsp;Vandana Joshi ,&nbsp;Markus Schweipert ,&nbsp;Obanna Pathur ,&nbsp;Kosana Sai Chaitanya ,&nbsp;Trinath Jamma ,&nbsp;Vivek Sharma ,&nbsp;Chandrasekhar Abbineni ,&nbsp;Franz-Josef Meyer-Almes ,&nbsp;Kondapalli Venkata Gowri Chandra Sekhar","doi":"10.1016/j.ejmcr.2025.100255","DOIUrl":"10.1016/j.ejmcr.2025.100255","url":null,"abstract":"<div><div>Traditional Histone deacetylase 8 (HDAC8) inhibitors primarily rely on hydroxamate-based scaffolds. However, there is a growing interest in developing non-hydroxamate inhibitors to overcome potential limitations with hydroxamate-based inhibitors. In this study, we report the design, synthesis, and evaluation of a series of benzyl-1,2,4-triazolo [4,3-a] pyridine derivatives as non-hydroxamate HDAC8 inhibitors. Their HDAC8 inhibitory activities were assessed by enzymatic assay. Active compounds from the HDAC8 enzymatic assay were evaluated in various cancer cell lines, revealing that compound <strong>9i</strong> demonstrated significant anti-neuroblastoma activity. Docking studies on compound <strong>9i</strong> were conducted to explicate its structural basis. The additional experiments showed that compound <strong>9i</strong> inhibited colony formation, induced hyperacetylation of SMC3, suppressed cell migration, triggered apoptosis, and caused cell cycle arrest in IMR-32 neuroblastoma cells. Overall, these inhibitors showed promising activity and a strong correlation with observed phenotypic effects, suggesting their potential for further development as therapeutic agents for cancer treatment.</div></div>","PeriodicalId":12015,"journal":{"name":"European Journal of Medicinal Chemistry Reports","volume":"13 ","pages":"Article 100255"},"PeriodicalIF":0.0,"publicationDate":"2025-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143548631","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Direct conversion of peptides into diverse peptidomimetics using a transformer-based chemical language model","authors":"Atsushi Yoshimori ,&nbsp;Jürgen Bajorath","doi":"10.1016/j.ejmcr.2025.100249","DOIUrl":"10.1016/j.ejmcr.2025.100249","url":null,"abstract":"<div><div>The design of pharmaceutically relevant compounds that mimic bioactive peptides or secondary structure elements in proteins is an important task in medicinal chemistry. Over time, various chemical strategies have been developed to convert natural peptide ligands into so-called peptidomimetics. This process is supported by computational approaches to identify peptidomimetic candidate compounds or design templates mimicking active peptide conformations. However, generating peptidomimetics continues to be challenging. Chemical language models (CLMs) offer new opportunities for molecular design. Therefore, we have revisited computational design of peptidomimetics from a different perspective and devised a CLM to directly transform input peptides into peptidomimetic candidates, without requiring intermediate states. A critically important aspect of the approach has been the generation of training data for effective learning that was guided by a quantitative measure of peptide-likeness such that the CLM could implicitly capture transitions from peptides or peptide-like molecules to compounds with reduced or eliminated peptide character. Herein, we introduce the CLM for peptidomimetics design and establish proof-of-principle for the approach. For given input peptides, both the general model and a version fine-tuned for a specific application were shown to produce a spectrum of candidate compounds with varying similarity, gradually changing chemical features, and diminishing peptide-likeness. As a part of our study, the CLM and data are provided.</div></div>","PeriodicalId":12015,"journal":{"name":"European Journal of Medicinal Chemistry Reports","volume":"13 ","pages":"Article 100249"},"PeriodicalIF":0.0,"publicationDate":"2025-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143160281","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Biological evaluation of novel 5-((1H-indol-3-yl) methyl)-2-(4-chlorobenzyl)-6-phenyl-imidazo[2,1-b][13,4]thiadiazole derivatives as novel BCL-2 specific inhibitors","authors":"Shivangi Sharma ,&nbsp;Sadashivamurthy Shamanth ,&nbsp;Humaira Siddiqua ,&nbsp;Laijau Goyary ,&nbsp;Kunigal S. Sagar ,&nbsp;Susmita Kumari ,&nbsp;Divya Sathees ,&nbsp;Gudapureddy Radha ,&nbsp;Bibha Choudhary ,&nbsp;Sathees C. Raghavan ,&nbsp;Kempegowda Mantelingu","doi":"10.1016/j.ejmcr.2025.100247","DOIUrl":"10.1016/j.ejmcr.2025.100247","url":null,"abstract":"<div><div>Antiapoptotic protein BCL2 is known to be upregulated in several cancer cells and therefore, it is an excellent target for cancer therapy. Previously, we reported a novel BCL2 inhibitor, Disarib, which inhibited BCL2 by predominantly binding to its BH1 domain and exhibited platelet-sparing ability like ABT199, the only FDA-approved BCL2 inhibitor. Here, we have synthesized the novel Disarib derivatives where oxindole moiety in Disarib was replaced with indole and evaluated their biological activity. We report several derivatives of Disarib and the identification of DSR 43 and 4-OCH₃, as the most potent among them. Treatment of cancer cell lines with the Disarib derivatives, DSR 43 and 4-OCH₃ led to the activation of the apoptotic pathway without generating any ROS or disrupting the mitochondrial membrane potential within the cells, leading to cell death. Western blot analysis in tandem with Annexin V/PI staining confirmed the activation of apoptosis. <em>In silico</em> studies, using derivatives suggests a promising therapeutic window with less off-target effects. Furthermore, their efficacy across different cancer cell lines highlights their broad potential as anticancer agents. Taken together, our results suggest that Disarib derivatives may have the potential to be developed as cancer therapeutic.</div></div>","PeriodicalId":12015,"journal":{"name":"European Journal of Medicinal Chemistry Reports","volume":"13 ","pages":"Article 100247"},"PeriodicalIF":0.0,"publicationDate":"2025-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143160279","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Synthesis and in vitro/in silico evaluation of the antimalarial activity of potential amino-quinoline derivatives","authors":"Moussa Touré ,&nbsp;Abdoulaye Gassama ,&nbsp;Oumar Sambou ,&nbsp;Christian Cavé ,&nbsp;Sandrine Cojean","doi":"10.1016/j.ejmcr.2024.100241","DOIUrl":"10.1016/j.ejmcr.2024.100241","url":null,"abstract":"<div><div>In this study, a series of <em>N</em>-arylamino-7-chloroquinolines were synthesized via an alkylation reaction involving aniline derivatives <strong>(2)</strong> and 4,7-dichloroquinoline <strong>(1)</strong>. Additionally, the synthesis of a library of <em>N</em>-aryl-<em>N</em>-benzylamino-7-chloroquinoline analogues, modified on the aniline nitrogen, has also reported. A structure-activity relationship (SAR) study was conducted to evaluate the biological efficacy and safety of these derivatives against chloroquine-sensitive (<em>Pf</em>3D7) and chloroquine-resistant (<em>Pf</em>W2) <em>Plasmodium falciparum</em> strains. Compounds <strong>5i</strong> and <strong>5c</strong> showed promising efficacy against the <em>Pf</em>3D7 strain with IC₅₀ values of 0.25 μM and 0.54 μM, respectively, while compound <strong>5l</strong> demonstrated significant activity against the <em>Pf</em>W2 strain with an IC₅₀ of 5.82 μM. The cytotoxicity of these compounds was also evaluated on HUVEC cell lines. Additionally, their pharmacological and pharmacokinetic (ADME) properties were studied to predict their fate and identify promising candidates for further clinical studies.</div></div>","PeriodicalId":12015,"journal":{"name":"European Journal of Medicinal Chemistry Reports","volume":"13 ","pages":"Article 100241"},"PeriodicalIF":0.0,"publicationDate":"2025-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143160325","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Synthesis, In vitro antimicrobial activity, and In silico bioinformatical approach of xanthone-fatty acid esters against Staphylococcus aureus, Escherichia coli, and Candida albicans","authors":"Yehezkiel Steven Kurniawan ,&nbsp;Ervan Yudha ,&nbsp;Jumina ,&nbsp;Harno Dwi Pranowo ,&nbsp;Eti Nurwening Sholikhah","doi":"10.1016/j.ejmcr.2025.100245","DOIUrl":"10.1016/j.ejmcr.2025.100245","url":null,"abstract":"<div><div>Microbial infection is gaining attention nowadays due to a high number of active cases and mortality rate. Because of that, research in finding new antimicrobial agents is urgently needed. In this work, we combined the chemical structure of 3-hydroxyxanthone and some fatty acids through ester linkage to form xanthyl laurate, xanthyl myristate, xanthyl palmitate, xanthyl stearate, and xanthyl oleate in 78.68–89.77 % yield. The <em>in vitro</em> antimicrobial assay revealed that xanthyl laurate exhibited the strongest antimicrobial activity with zone of inhibition of 11.0 ± 1.65, 9.43 ± 1.74, and 9.30 ± 1.37 mm against <em>Staphylococcus aureus</em>, <em>Escherichia coli</em>, and <em>Candida albicans</em>, respectively, which also higher than 3-hydoxyxanthone and lauric acid. Xanthyl laurate also yielded minimum inhibition concentration values of 31.25–62.50 μg/mL, which was 2 times lower than of 3-hydroxyxanthone. The structure-based bioinformatical approach indicated that ftsZ <em>S. aureus</em>, MAPK <em>E. coli</em>, and PDE <em>C. albicans</em> are the potential target for xanthyl laurate. Furthermore, both molecular docking and molecular dynamic simulations indicated good stability of xanthyl laurate in the active site of each protein receptor through hydrogen bond and other non-covalent interactions. The <em>in vitro</em> cytotoxicity assay against the NIH3T3 cell line showed that xanthyl laurate was non-toxic at 500 μg/mL with a cell viability percentage of 86.14 ± 1.38 %. This study reports that xanthyl laurate is the most potential antimicrobial agent based on the xanthone-fatty acid ester's structure against <em>S. aureus</em>, <em>E. coli</em>, and <em>C. albicans</em> in both <em>in vitro</em> and <em>in silico</em> assays.</div></div>","PeriodicalId":12015,"journal":{"name":"European Journal of Medicinal Chemistry Reports","volume":"13 ","pages":"Article 100245"},"PeriodicalIF":0.0,"publicationDate":"2025-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143160277","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Indoles in drug design and medicinal chemistry","authors":"Benjamin A. Babalola ,&nbsp;Monika Malik ,&nbsp;Olanike Olowokere ,&nbsp;Ayomide Adebesin ,&nbsp;Lekhnath Sharma","doi":"10.1016/j.ejmcr.2025.100252","DOIUrl":"10.1016/j.ejmcr.2025.100252","url":null,"abstract":"<div><div>Indole derivatives represent a significant class of compounds in medicinal chemistry due to their diverse biological activities and structural versatility. These compounds are central to the design of drugs targeting a wide array of diseases, including cancer, diabetes, cardiovascular disorders, neurological diseases, and infections. The indole scaffold facilitates interactions with biological macromolecules, enhancing its utility in drug development. This review summarizes the latest advancements in the synthesis, biological efficacy, and therapeutic potential of indole derivatives. Classical methods, such as Fischer, Bartoli, and Reissert indole synthesis, continue to serve as foundational techniques, while modern advancements in combinatorial methods, transition-metal catalysis, cyclization methods, nanoparticles-mediated synthesis, heterogenous catalysis, microwave-aided catalysis, ultrasound-aided approach, and green chemistry offer more efficient, sustainable approaches. Notably, indole derivatives exhibit potent antifungal, antiprotozoal, antidiabetic, antioxidant, antimalarial, antibacterial, anti-inflammatory, and anticancer activities. Recent studies highlight the role of structural modifications in optimizing these compounds for enhanced pharmacological outcomes. For instance, indole-triazole conjugates show impressive antifungal activity, while indole-thiazolidine-2,4-dione inhibitors exhibit strong antidiabetic effects. Additionally, indole derivatives have demonstrated efficacy in targeting key oncogenic pathways, with some compounds exhibiting potent anticancer properties against various cell lines. These promising findings are supported by computational modelling studies that reveal strong interactions with target proteins. Emerging trends in indole-based drug discovery, including the integration of computational modelling and molecular docking, are expected to drive the development of next-generation therapeutics. As research in this area progresses, indole derivatives are poised to remain integral to the development of innovative treatments for a broad range of diseases.</div></div>","PeriodicalId":12015,"journal":{"name":"European Journal of Medicinal Chemistry Reports","volume":"13 ","pages":"Article 100252"},"PeriodicalIF":0.0,"publicationDate":"2025-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143463783","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}