{"title":"Profiling and cheminformatics bioprospection of curcurbitacin I and momordin Ic from <i>Momordica balsamina</i> on α-amylase and α-glucosidase.","authors":"Viruska Jaichand, Adedayo Ayodeji Lanrewaju, Himansu Baijnath, Saheed Sabiu, Viresh Mohanlall","doi":"10.1080/14756366.2025.2492706","DOIUrl":"https://doi.org/10.1080/14756366.2025.2492706","url":null,"abstract":"<p><p><i>Momordica</i> spp. has been traditionally used to manage type 2 diabetes mellitus, but the mechanisms and metabolites remain unclear. This study evaluated the inhibitory potential of Momordica <i>balsamina</i> extracts on α-amylase and α-glucosidase <i>in vitro</i>, identifying cucurbitacin I and momordin Ic via high-performance liquid chromatography-photo diode array, and their inhibitory potential <i>in silico</i>. Ethyl acetate seed extract (14.46 µg/ml) and hexane fruit flesh extract (16.79 µg/ml) exhibited lower IC<sub>50</sub> values against α-amylase and α-glucosidase, respectively, compared to acarbose (reference standard). Comparatively, momordin Ic concentrations (36.57-605.98 µg/ml) were higher than cucurbitacin I (17.08-44.34 µg/ml). A 140 ns simulation showed that cucurbitacin I (-63.06 kcal/mol) and momordin Ic (-66.53 kcal/mol) exhibited stronger binding to α-amylase than acarbose (-36.46 kcal/mol), whereas cucurbitacin I (-38.08 kcal/mol) and momordin Ic (-54.87 kcal/mol) displayed weaker binding to α-glucosidase, relative to acarbose (-63.73 kcal/mol). Generally, momordin Ic demonstrated better thermodynamic properties, hence further <i>in vitro</i> and <i>in vivo</i> studies are needed to validate their antidiabetic potential.</p>","PeriodicalId":15769,"journal":{"name":"Journal of Enzyme Inhibition and Medicinal Chemistry","volume":"40 1","pages":"2492706"},"PeriodicalIF":5.6,"publicationDate":"2025-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12044915/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144022271","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Activity guided discovery of dual inhibitors of α-glucosidase and β-glucuronidase from the leaves of <i>Millettia pachycarpa</i> Benth.","authors":"Yanxi He, Huanran Xu, Shaoqian Tan, Jing Long, Hui Lei, Ling Xiao, Xiaoyi Qi, Mingming Deng, Xia Xiong, Jingcan You, Liangliang Zhu, Muhan Lü, Sicheng Liang","doi":"10.1080/14756366.2025.2501041","DOIUrl":"10.1080/14756366.2025.2501041","url":null,"abstract":"<p><p>Type 2 diabetes mellitus (T2DM) and cancers are two globally prevalent diseases which can increase the incidence of each other. Intestinal α-glucosidase and β-glucuronidase are key targets for glycaemic control and chemotherapy detoxification, respectively. This study first found that the leaf methanol extract of <i>Millettia pachycarpa</i> displayed dual inhibition to the two enzymes. The dually active constituents were then isolated and identified as two prenylated isoflavones of 6,8-diprenylorobol and 6,8-diprenylgenistein. Diprenylorobol exhibits competitive inhibition to both the two enzymes with <i>K<sub>i</sub></i> values of 21.6 μM (α-glucosidase) and 1.41 μM (β-glucuronidase). Diprenylgenistein is an uncompetitive inhibitor of α-glucosidase (<i>K<sub>i</sub></i> = 11.4 μM) but a competitive inhibitor of β-glucuronidase (<i>K<sub>i</sub></i> = 1.69 μM). Molecular docking studies showed that both the two isoflavones tightly bind into the active pockets via various hydrogen bonds and hydrophobic interactions. In summary, the current study identifies two promising dual inhibitors of α-glucosidase and β-glucuronidase from the leaves of <i>Millettia pachycarpa</i>.</p>","PeriodicalId":15769,"journal":{"name":"Journal of Enzyme Inhibition and Medicinal Chemistry","volume":"40 1","pages":"2501041"},"PeriodicalIF":5.6,"publicationDate":"2025-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12082738/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144078334","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
José L Pereira Filho, Renato B Pereira, Tatiana F Vieira, Sérgio F Sousa, José R A Coelho, Nuno F S Pinto, Catarina M M Coelho, Maria José G Fernandes, Elisabete M S Castanheira, Maria S T Gonçalves, David M Pereira
{"title":"Development of eugenol derivatives with 5-LOX inhibitory activity.","authors":"José L Pereira Filho, Renato B Pereira, Tatiana F Vieira, Sérgio F Sousa, José R A Coelho, Nuno F S Pinto, Catarina M M Coelho, Maria José G Fernandes, Elisabete M S Castanheira, Maria S T Gonçalves, David M Pereira","doi":"10.1080/14756366.2025.2535586","DOIUrl":"https://doi.org/10.1080/14756366.2025.2535586","url":null,"abstract":"<p><p>Eugenol (4-allyl-2-methoxyphenol), is the major chemical constituent in the essential oil of numerous plant species. Several biological properties have been described for this molecule, including modulation of enzymatic targets relevant for the inflammatory response, such as 5-lipoxygenase (5-LOX). As so, there is interest in expanding the chemical space of this molecule to develop new molecules to be used in inflammatory conditions. We describe the chemometric analysis of several eugenol derivatives, which show that the chemical space of the parent molecule was successfully expanded. All molecules were evaluated for their inhibition towards 5-LOX, an important player in inflammatory pathways. Four derivatives exhibited significant 5-LOX inhibitory activity, which prompted further studies. The most promising compounds, 4-allylbenzene-1,2-diol <b>2</b>, ethyl-4-(4-allyl-2-methoxyphenoxy)butanoate <b>4e</b>, 3-(2-methoxy-4-(oxiran-2-ylmethyl)phenoxy)propyl acetate <b>5d</b> and 4-(3-(<i>tert</i>-butoxy)-2-hydroxypropyl)-2-methoxyphenol <b>7c</b>, were submitted to <i>in silico</i> assays to validate their affinity and stability towards 5-LOX, which helped clarify the mechanism by which these molecules interact and inhibit this enzyme.</p>","PeriodicalId":15769,"journal":{"name":"Journal of Enzyme Inhibition and Medicinal Chemistry","volume":"40 1","pages":"2535586"},"PeriodicalIF":5.4,"publicationDate":"2025-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12377105/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144956587","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Inhibition of 12/15-LOX hyperactivation mitigates cognitive decline in a chronic cerebral hypoperfusion mouse model and in H<sub>2</sub>O<sub>2</sub>-induced HT22 cells: therapeutic effects of brozopine.","authors":"Xuening Wang, Zhizai Lu, Qiuji Shao, Yi Wang, Zixin Zhang, Zhiyu Wang, Qingran Jia, Jinpeng Zhu, Yiran Song, Lingxu Yuan, Yiming Wang, Shaoyang Xu, Lirou He, Junbiao Chang, Yuan Gao","doi":"10.1080/14756366.2025.2547259","DOIUrl":"https://doi.org/10.1080/14756366.2025.2547259","url":null,"abstract":"<p><p>Brozopine (BZP), a novel inhibitor of 12/15-lipoxygenase (12/15-LOX), has previously demonstrated efficacy in mitigating inflammatory and oxidative stress-related injury in cerebral ischaemia models. This study aimed to evaluate the therapeutic potential and underlying mechanisms of BZP in a mouse model of vascular dementia induced by chronic cerebral hypoperfusion. BZP was administered for 28 days following right unilateral common carotid artery occlusion (rUCCAO) in mice. BZP significantly alleviated cognitive impairment, behavioural deficits, and fine motor function. Mechanistically, BZP inhibited 12/15-LOX, cPLA<sub>2</sub>, p-p38 MAPK/p38 MAPK ratio, tumour necrosis factor-α, interlukin-1β, Aβ<sub>1-42</sub> deposition, and Tau hyperphosphorylation in the brain and serum of rUCCAO mice. Similar protective effects were observed in both 12/15-LOX-overexpressed and H<sub>2</sub>O<sub>2</sub>-induced HT22 cell models. These findings suggest that BZP exerts its neuroprotective effects by targeting the 12/15-LOX/cPLA<sub>2</sub>/p38 MAPK pathway, offering a promising therapeutic strategy for mitigating the progression of cognitive impairment.</p>","PeriodicalId":15769,"journal":{"name":"Journal of Enzyme Inhibition and Medicinal Chemistry","volume":"40 1","pages":"2547259"},"PeriodicalIF":5.4,"publicationDate":"2025-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12372482/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144956637","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Amira Mira, Fatma M Abdel Bar, Ahmed I Foudah, Mohamed H Aboutaleb, Tarek S Ibrahim, Ahmed H E Hassan, Ashraf T Khalil
{"title":"Bio-guided discovery of antibacterial metabolites from <i>Penicillium chrysogenum</i>.","authors":"Amira Mira, Fatma M Abdel Bar, Ahmed I Foudah, Mohamed H Aboutaleb, Tarek S Ibrahim, Ahmed H E Hassan, Ashraf T Khalil","doi":"10.1080/14756366.2025.2547258","DOIUrl":"https://doi.org/10.1080/14756366.2025.2547258","url":null,"abstract":"<p><p>Bio-guided isolation from the Red Sea-derived <i>Penicillium chrysogenum</i> yielded two new metabolites, 15-deoxy-15-amino-citreohybridonol (<b>6</b>) and chrysogenotoxin (<b>7</b>), alongside five known compounds: emodin (<b>1</b>), chrysophanol (<b>2</b>), <i>bis</i>(2-ethylhexyl) phthalate (<b>3</b>), haenamindole (<b>4</b>), and citreorosein (<b>5</b>). Compound <b>6</b> exhibited broad-spectrum antibacterial activity against both Gram-positive (MIC: 0.31-0.62 μM; MBC: 0.31-0.62 μM) and Gram-negative bacteria (MIC: 0.15-1.25 μM; MBC: 0.62-2.5 μM). Compound <b>7</b> showed potent bactericidal activity against Gram-negative bacteria (MIC: 0.07-0.31 μM; MBC: 0.15-0.62 μM) with MBC/MIC ≤ 4, while compound <b>4</b> selectively inhibited <i>S. pneumoniae</i> (MIC: 0.31 μM; MBC: 0.62 μM). Compounds <b>4</b>, <b>6</b>, and <b>7</b> exhibited low cytotoxicity towards human intestinal epithelial cells (HIEC-6). Molecular docking studies targeting the NDM-1 β-lactamase identified compounds <b>4</b>, <b>6</b>, and <b>7</b> as potential inhibitors of New Delhi metallo-β-lactamase-1 (NDM-1). Molecular dynamics simulations confirmed the structural stability of <b>7</b> within the NDM-1 active site. Chrysogenotoxin (<b>7</b>) was suggested as a promising antibacterial candidate against antibiotic-resistant pathogens.</p>","PeriodicalId":15769,"journal":{"name":"Journal of Enzyme Inhibition and Medicinal Chemistry","volume":"40 1","pages":"2547258"},"PeriodicalIF":5.4,"publicationDate":"2025-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12381984/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144956667","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Jason H Gill, Jonathan D Sellars, Paul G Waddell, Steven D Shnyder, Ronald Grigg, Colin W G Fishwick
{"title":"Development of novel benzamide class I selective lysine deacetylase inhibitors as potent anticancer agents.","authors":"Jason H Gill, Jonathan D Sellars, Paul G Waddell, Steven D Shnyder, Ronald Grigg, Colin W G Fishwick","doi":"10.1080/14756366.2025.2520612","DOIUrl":"10.1080/14756366.2025.2520612","url":null,"abstract":"<p><p>Small molecule inhibitors of lysine deacetylases (KDACs), exemplified by histone deacetylases (HDACs), exhibit significant promise as cancer therapeutics. Using a modular combinatorial chemistry approach, a novel class of KDAC inhibitors (KDACi) containing the aminophenyl-benzamide headgroup have been developed, which incorporate a vinyl group within the linker region for active site stabilisation and a trifluoromethyl moiety within the capping group to exploit enzyme surface topology. Consequently, a class I selective KDACi (<b>7</b>) with a preference towards HDAC1 over other class I KDACs was identified. This KDACi orientates differently within the KDAC active site and exhibits an improved antitumour profile relative to the benchmark class I selective KDACi Entinostat (<b>1</b>). The clinical potential of <b>7</b> is further exemplified by the inhibition of tumour growth in an <i>in vivo</i> model of ovarian cancer. These results offer significant scope for the rational development of KDACi with improved selectivity against specific KDAC and widespread therapeutic potential.</p>","PeriodicalId":15769,"journal":{"name":"Journal of Enzyme Inhibition and Medicinal Chemistry","volume":"40 1","pages":"2520612"},"PeriodicalIF":5.6,"publicationDate":"2025-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12217109/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144540460","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Nazar Trotsko, Agnieszka Głogowska, Barbara Kaproń, Katarzyna Kozieł, Ewa Augustynowicz-Kopeć, Agata Paneth
{"title":"The new thiazolidine-2,4-dione-based hybrids with promising antimycobacterial activity: design, synthesis, biological evaluation, and drug interaction analysis.","authors":"Nazar Trotsko, Agnieszka Głogowska, Barbara Kaproń, Katarzyna Kozieł, Ewa Augustynowicz-Kopeć, Agata Paneth","doi":"10.1080/14756366.2024.2442703","DOIUrl":"https://doi.org/10.1080/14756366.2024.2442703","url":null,"abstract":"<p><p>The ever-increasing drug-resistant tuberculosis (TB) has invigorated the focus on the discovery and development of novel therapeutic agents and treatment options. Thiazolidinone-based compounds have shown good antitubercular properties <i>in vitro</i>. Here, we report the design and synthesis of a number of new derivatives inspired by the structure of thiazolidine-2,4-dione (TZD). The TZD-based hybrids with the thiosemicarbazone or the pyridinecarbohydrazone moiety were synthesised and their antimycobacterial activity was investigated against the reference H<sub>37</sub>Rv and two wild <i>Mycobacterium tuberculosis</i> (<i>Mtb</i>) strains. In further studies, a two-drug interaction analysis was also performed for assessing their synergism with the current first-line drugs used for the treatment of TB. It was found that some of the compounds showed high antimycobacterial activity with MICs (0.078-0.283 µM) and a synergistic effect with isoniazid or rifampicin, thereby demonstrating their potential as a promising scaffold for the development of novel coadjuvants for the effective treatment of TB.</p>","PeriodicalId":15769,"journal":{"name":"Journal of Enzyme Inhibition and Medicinal Chemistry","volume":"40 1","pages":"2442703"},"PeriodicalIF":5.6,"publicationDate":"2025-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142921572","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":"Liquidambaric acid as a non-competitive α-glucosidase inhibitor: multi-level evidence from enzyme kinetics, molecular docking, molecular dynamics simulations, and a <i>Drosophila</i> hyperglycaemic model.","authors":"Liwei Jia, Yan Liu, Bo Fu, Yuan Tian, Xin Meng","doi":"10.1080/14756366.2025.2497486","DOIUrl":"https://doi.org/10.1080/14756366.2025.2497486","url":null,"abstract":"<p><p>Liquidambaric acid, a pentacyclic triterpenoid from <i>Liquidambar formosana Hance</i>, was evaluated as a novel α-glucosidase inhibitor for type 2 diabetes mellitus (T2DM) management. Enzyme kinetic assays revealed its potent non-competitive inhibition (IC<sub>50</sub> = 0.12 mM). Molecular docking showed stable hydrogen bonding at an allosteric site, altering enzyme conformation, while 100 ns molecular dynamics (MD) simulations confirmed the stability of the protein-ligand complex. <i>In vivo</i>, a <i>Drosophila melanogaster</i> hyperglycaemic model demonstrated significant glucose reduction, confirming its hypoglycaemic potential. ADMET analysis predicted favourable bioavailability and low toxicity, supporting its development as a safe therapeutic agent. These findings integrate enzyme kinetics, molecular modelling, MD simulations, and <i>in vivo</i> validation, highlighting liquidambaric acid's potential as a multifunctional and cost-effective agent for T2DM management.</p>","PeriodicalId":15769,"journal":{"name":"Journal of Enzyme Inhibition and Medicinal Chemistry","volume":"40 1","pages":"2497486"},"PeriodicalIF":5.6,"publicationDate":"2025-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12044908/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143985791","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Meng Ning, Xiao-Cui Liu, Min He, Xing-Rong Peng, Ming-Hua Qiu
{"title":"2,5-Dihydroxyphenylethanone: an anti-melanogenic bioactive compound isolated from <i>Ganoderma cochlear</i>.","authors":"Meng Ning, Xiao-Cui Liu, Min He, Xing-Rong Peng, Ming-Hua Qiu","doi":"10.1080/14756366.2025.2495364","DOIUrl":"https://doi.org/10.1080/14756366.2025.2495364","url":null,"abstract":"<p><p>2,5-dihydroxyacetophenone, a natural product from the fruiting bodies of <i>Ganoderma cochlear</i>, can effectively and safely inhibit the production of melanin in zebrafish model. To achieve analogues with more significant inhibition, 9 analogs were synthesised and 13 analogues were purchased commercially. Among them, 14 compounds can inhibit melanin production, of which 5 compounds displayed the most significant inhibitory effects, with inhibitory rates of more than 80%, compared to positive control SymWhite<sup>®</sup>377 (phenylethyl resorcinol). This study elucidated the melanin-inhibitory effects of 2,5-dihydroxyacetophenone and its analogs, providing a theoretical foundation for their potential applications in anti-melanogenic reagents.</p>","PeriodicalId":15769,"journal":{"name":"Journal of Enzyme Inhibition and Medicinal Chemistry","volume":"40 1","pages":"2495364"},"PeriodicalIF":5.6,"publicationDate":"2025-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12044912/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143967843","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Identification of broad-spectrum M<sup>pro</sup> inhibitors: a focus on high-risk coronaviruses and conserved interactions.","authors":"Man Liu, Li Zhao, Xupeng Huang, Zhenhao Tang, Yihang Zhong, Mengrong Yan, Shun Liu, Shunjing Wang, Zeyun Sun, Zixuan Rao, Linyi Yu, Yuying Fang, Wei Zhang, Hongbo Zhang, Wei Peng","doi":"10.1080/14756366.2025.2503961","DOIUrl":"10.1080/14756366.2025.2503961","url":null,"abstract":"<p><p>The COVID-19 pandemic underscores the urgent need to develop broad-spectrum antivirals against coronaviruses (CoVs) to prepare for future outbreaks. In this study, we presented a systematic approach to developing broad-spectrum M<sup>pro</sup> inhibitors, with a focus on high-risk CoVs. We optimised <b>S-217622</b> as a lead compound, with the goal of enhancing conserved interactions within the S1, S2, and S3/S4 pockets of M<sup>pro</sup>, leading to significantly improved inhibitory potency against representative CoVs. Compound <b>25</b> exhibited submicromolar activity across all ten CoVs, with IC<sub>50</sub> values below 0.1 μM for six of them. The X-ray co-crystal structure of SARS-CoV-2 M<sup>pro</sup> in complex with compound <b>25</b> revealed the structural basis of conserved interactions contributing to its broad-spectrum activity. This study demonstrates the feasibility of reinforcing conserved interactions to develop M<sup>pro</sup> inhibitors with broad-spectrum activity and provides valuable strategies for combating future pandemics caused by unknown CoVs.</p>","PeriodicalId":15769,"journal":{"name":"Journal of Enzyme Inhibition and Medicinal Chemistry","volume":"40 1","pages":"2503961"},"PeriodicalIF":5.6,"publicationDate":"2025-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12096674/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144110509","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}