In silico pharmacology最新文献

{"title":"In-silico-based lead optimization of hit compounds targeting mitotic kinesin Eg5 for cancer management.","authors":"Damilola S Bodun, Damilola A Omoboyowa, Victor F Olofinlade, Adeyemi O Ayodeji, Andrea Mauri, Uchechukwu C Ogbodo, Toheeb A Balogun","doi":"10.1007/s40203-024-00300-6","DOIUrl":"https://doi.org/10.1007/s40203-024-00300-6","url":null,"abstract":"<p><p>Lead optimization is vital for turning hit compounds into therapeutic drugs. This study builds upon a prior in silico research, where the hit compounds had better binding affinity and stability compared to a reference drug. Using a genetic algorithm, 12,500 analogs of the top compounds from the prior study were generated. Virtual screening was done using a quantitative structure-activity relationship (QSAR) model. Top analogs, selected based on pChembL values below 6.000nM, underwent molecular docking targeting Human Eg5. The top five analogs from this study (Compound 9794, Compound 8592, Compound 9786, Compound 2744, and Compound 3246) demonstrated strong binding energies and interactions with key amino acids (GLU 116, GLU 117, and ARG 119). MMGBSA analysis revealed comparable affinities to the co-crystallized ligand, suggesting the top analogs' potential as Human Eg5 inhibitors. Induced fit docking highlighted Compound 9786's superior efficacy. Quantum Polarized Ligand Docking indicated promising scores for Compounds 8592 and 9786. ADMET predictions offered insights into pharmacological properties, with all compounds predicted to be HIA-positive and non-carcinogenic. Further MD simulation study confirms the stability of the top compounds in the active site of Eg5. This study shows the significance of integrated strategies in drug design. However, in vitro and in vivo studies should be conducted for these promising candidates to confirm their efficacy as Eg5 inhibitors.</p><p><strong>Supplementary information: </strong>The online version contains supplementary material available at 10.1007/s40203-024-00300-6.</p>","PeriodicalId":94038,"journal":{"name":"In silico pharmacology","volume":"13 1","pages":"9"},"PeriodicalIF":0.0,"publicationDate":"2025-01-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11703796/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142960492","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":"Unveiling structural components of dibenzofuran-based MMP-12 inhibitors: a comparative classification-dependent analysis with molecular docking-based virtual screening and molecular dynamics simulation.","authors":"Jigme Sangay Dorjay Tamang, Suvankar Banerjee, Balaram Ghosh, Sandip Kumar Baidya, Tarun Jha, Nilanjan Adhikari","doi":"10.1007/s40203-024-00296-z","DOIUrl":"https://doi.org/10.1007/s40203-024-00296-z","url":null,"abstract":"<p><p>The implication of matrix metalloproteinase-12 (MMP-12) in various major disorders including cancer, COPD, cardiovascular disorders, and neurological diseases makes it a potential target for drug discovery. Contemplating the significance of MMP-12, a number of MMP-12 inhibitors were designed, synthesized and tested throughout the world but the non-selective nature of most of those molecules can lead to adverse drug interactions. In contradiction, the dibenzofuran (DBF) and dibenzothiophene (DBT) derivatives showed highly potent and selective MMP-12 inhibition. Therefore, to identify the prime molecular and structural attributes that are affecting the MMP-12 inhibitory activity, the linear discriminant analysis (LDA), Bayesian classification, recursive partitioning, and SARpy analysis were performed to extract the prime attributes of these DBFs and DBTs affecting MMP-12 inhibition. These studies suggested that substructures like isopropyl carboxylic acid, 5-methyl furan, 1,2,4-oxadiazole, and DBT moieties can impart moderate to high contribution for MMP-12 inhibition. Importantly, the outcomes of the current studies were also in agreement with our regression-based study performed earlier. Furthermore, the molecular docking-mediated virtual screening of DBT and DBF analogs of the ChEMBL database demonstrated the viability of other DBT and DBF analogs to become potential MMP-12-selective inhibitors. The molecular dynamics (MD) simulation study of hit molecules also showed the potential of the combination of phosphonic acid ZBG and DBF P1' substituent for effective anchoring/binding at the MMP-12 active site. Therefore, the findings may help in the discovery and designing of novel MMP-12 inhibitors that may be used for the treatment of various pathological diseases including cancer and COPD.</p><p><strong>Supplementary information: </strong>The online version contains supplementary material available at 10.1007/s40203-024-00296-z.</p>","PeriodicalId":94038,"journal":{"name":"In silico pharmacology","volume":"13 1","pages":"10"},"PeriodicalIF":0.0,"publicationDate":"2025-01-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11704098/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142960494","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":"Structure similarity based screening coupled to integrated structural biochemistry approach for exploring the high affinity inhibitors against histone deacetylase (HDAC)-6.","authors":"Shabir Ahmad Ganai, Suma Mohan","doi":"10.1007/s40203-024-00294-1","DOIUrl":"https://doi.org/10.1007/s40203-024-00294-1","url":null,"abstract":"<p><p>Histone deacetylase (HDAC)-6 has overwhelming implications in multiple cancers and neurodegenerative disorders. Unusual HDAC6 expression modulates various signalling mechanisms which in turn forms the aetiology of the above-mentioned disorders. Thus, restoring the typical activity of HDAC6 through small molecules may prove as a promising approach to beat these disorders. Herein, we employed an integrated approach for exploring the high binding affinity manifesting molecules against HDAC6. We screened the entire PubChem database using Tubastatin A as the reference (query) molecule following which we carried out 110 molecular docking (XP-mode) and 110 MM-GBSA experiments. Thirty-three molecules demonstrated raised binding affinity than query in the HDAC6 active site. Further, the top 3 binders selected on logical grounds were subjected to interaction study, two hit molecules and tubastatin-A were subjected to convoluted molecular dynamics and three-dimensional e-Pharmacophores mapping was done to delineate the rationale behind the high binding tendency of hit molecules over control molecule. This work provides a solid foundation for additional research towards the development of lead molecules from the said hits for therapeutic intervention against HDAC6 overexpression-driven disorders.</p>","PeriodicalId":94038,"journal":{"name":"In silico pharmacology","volume":"13 1","pages":"8"},"PeriodicalIF":0.0,"publicationDate":"2025-01-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11695532/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142934236","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":"Exploring the efficacy of some biologically active compounds as anti-hypertensive drugs: an insightful evaluation through DFT, molecular docking and molecular dynamics simulations.","authors":"Sourav Majumdar, Anup Pramanik","doi":"10.1007/s40203-024-00291-4","DOIUrl":"10.1007/s40203-024-00291-4","url":null,"abstract":"<p><p>Among different anti-hypertensive drugs, calcium channel blockers and human angiotensin-converting enzyme (ACE) inhibitors are the two main types. Herein, we took 25 biologically active ligands with potent anti-hypertensive activities and performed molecular docking studies with the human ACE receptor (PDB ID 1O8A) and human leukocyte antigens (HLA) complex, human voltage-dependent calcium channel alpha1 subunit (PDB ID 3LV3). Beforehand, we had performed density functional theory (DFT) studies to find out their structure-property relationships. In-silico ADMET studies were conducted, and we found that all 25 ligands follow Lipinski's Rule of 5, which confirms their oral bioavailability and high gastrointestinal absorption as a drug. Finally, molecular dynamics (MD) simulation studies were performed for the two top-scored drugs for 100 ns which reveal that a strong influence of the ligand (flunarizine) is there over the respective proteins.</p><p><strong>Supplementary information: </strong>The online version contains supplementary material available at 10.1007/s40203-024-00291-4.</p>","PeriodicalId":94038,"journal":{"name":"In silico pharmacology","volume":"13 1","pages":"4"},"PeriodicalIF":0.0,"publicationDate":"2024-12-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11668705/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142901436","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":"In silico design and assessment of a multi-epitope peptide vaccine against multidrug-resistant <i>Acinetobacter baumannii</i>.","authors":"Shiv Nandan Sah, Sumit Gupta, Neha Bhardwaj, Lalit Kumar Gautam, Neena Capalash, Prince Sharma","doi":"10.1007/s40203-024-00292-3","DOIUrl":"10.1007/s40203-024-00292-3","url":null,"abstract":"<p><p><i>Acinetobacter baumannii</i>, an opportunistic and notorious nosocomial pathogen, is responsible for many infections affecting soft tissues, skin, lungs, bloodstream, and urinary tract, accounting for more than 722,000 cases annually. Despite the numerous advancements in therapeutic options, no approved vaccine is currently available for this particular bacterium. Consequently, this study focused on creating a rational vaccine design using bioinformatics tools. Three outer membrane proteins with immunogenic potential and properties of good vaccine candidates were used to select epitopes based on good antigenic properties, non-allergenicity, high binding scores, and a low IC50 value. A multi-epitope peptide (MEP) construct was created by sequentially linking the epitopes using suitable linkers. ClusPro 2.0 and C-ImmSim web servers were used for docking analysis with TLR2/TLR4 and immune response respectively. The Ramachandran plot showed an accurate model of the MEP with 100% residue in the most favored and allowed regions. The construct was highly antigenic, stable, non-allergenic, non-toxic, and soluble, and showed maximum population coverage. Additionally, molecular docking demonstrated strong binding between the designed MEP vaccine and TLR2/TLR4. In silico immunological simulations showed significant increases in T-cell and B-cell populations. Finally, codon optimization and in silico cloning were conducted using the pET-28a (+) plasmid vector to evaluate the efficiency of the expression of vaccine peptide in the host organism (<i>Escherichia coli</i>). This designed MEP vaccine would support and accelerate the laboratory work to develop a potent vaccine targeting MDR <i>Acinetobacter baumannii</i>.</p><p><strong>Supplementary information: </strong>The online version contains supplementary material available at 10.1007/s40203-024-00292-3.</p>","PeriodicalId":94038,"journal":{"name":"In silico pharmacology","volume":"13 1","pages":"7"},"PeriodicalIF":0.0,"publicationDate":"2024-12-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11668725/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142901437","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":"Repurposing fluvoxamine as an inhibitor for NUDT5 in breast cancer cell: an in silico and in vitro study.","authors":"Sumathi Ramasamy, Kanimozhi Jeyaram, Aathimoolam Narayanan, Sankarganesh Arunachalam, Selvarajan Ethiraj, Muthumanickam Sankar, Boomi Pandian","doi":"10.1007/s40203-024-00293-2","DOIUrl":"10.1007/s40203-024-00293-2","url":null,"abstract":"<p><p>Drug repurposing is necessary to accelerate drug discovery and meet the drug needs. This study investigated the possibility of using fluvoxamine to inhibit the cellular metabolizing enzyme NUDT5 in breast cancer. Computational and experimental techniques were used to evaluate the structural flexibility, binding stability, and chemical reactivity of the drugs. These findings indicated that fluvoxamine effectively suppressed the activity of NUDT5, as evidenced by a binding score of - 8.514 kcal/mol. Furthermore, the binding positions of fluvoxamine and NUDT5 were optimized. Fluvoxamine attachment to the active sites of Trp28, Trp46, Glu47, Arg51, Arg84, and Leu98 in NUDT5 has been shown to alter the metabolism of ADPr. These alterations play a role in ATP production in the breast cancer cells. In addition, an MTT assay conducted on the MCF-7 cell line using fluvoxamine revealed an IC50 value of 53.86 ± 0.05 µM. Fluvoxamine-induced apoptosis was confirmed as evidenced by AO/EtBr and DAPI staining.</p><p><strong>Graphical abstract: </strong>Effect of fluvoxamine on breast cancer cells.</p>","PeriodicalId":94038,"journal":{"name":"In silico pharmacology","volume":"13 1","pages":"5"},"PeriodicalIF":0.0,"publicationDate":"2024-12-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11668718/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142899920","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":"Network pharmacology-integrated molecular modeling analysis of <i>Aquilaria malaccensis</i> L. (agarwood) essential oil phytocompounds.","authors":"Prajisha Jayaprakash, Twahira Begum, Mohan Lal","doi":"10.1007/s40203-024-00289-y","DOIUrl":"10.1007/s40203-024-00289-y","url":null,"abstract":"<p><p>A network pharmacology approach was used to construct comprehensive pharmacological networks, elucidating the interactions between agarwood compounds and key biological targets associated with cancer pathways. We have employed a combination of network pharmacology, molecular docking and molecular dynamics to unravel agarwood plants' active components and potential mechanisms. Reported 23 molecules were collected from the agarwood plants and considered to identify molecular targets. Further, we identified ten potent targets related to cancer through network pharmacology analysis. The key targets include EGFR, JUN, TP53, SRC, MAPK3, ACTB, GAPDH, AKT1, MYC and CTNNB1. The biological processes include the negative regulation of fibroblast proliferation, metabolic, oxidative, and more. Subsequently, molecular docking results have indicated that 7-isopropenyl-1, 4a-dimethyl-4, 4a, 5,6,7,8-hexahydro-3 H-naphthalen-2-one showed an excellent binding affinity for all ten targets. This is the first study; we employed a novel integrated approach that combines network pharmacology, molecular docking and molecular dynamics simulation (MDS). The GO and KEGG, pathway enrichment analyses, shed light on biological processes relevant to cancer treatment. Moreover, molecular docking studies results indicated that the molecule 7-isopropenyl-1,4a-dimethyl-4,4a,5,6,7,8-hexahydro-3H-naphthalen-2-one exhibited strong binding affinity among all ten cancer targets, with a docking score ranging from - 9.9 to - 6.7 kcal/mol and found to have hydrogen bond interaction with Lys168, Ser322, Thr336 and Ala946 residues. MDS sheds light on the stability of their binding, the longevity of their interactions, and their overall effect on the enzyme's active site throughout the simulation. The current work signifies the initial report using bioinformatics approaches to assess the anticancer properties of compounds derived from the agarwood plant.</p>","PeriodicalId":94038,"journal":{"name":"In silico pharmacology","volume":"13 1","pages":"3"},"PeriodicalIF":0.0,"publicationDate":"2024-12-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11668724/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142901439","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":"In vitro and in silico approaches manifest the anti-leishmanial activity of wild edible mushroom <i>Amanita princeps</i>.","authors":"Ishita Bhattacharya, Nibedita Pyne, Santanu Paul","doi":"10.1007/s40203-024-00287-0","DOIUrl":"10.1007/s40203-024-00287-0","url":null,"abstract":"<p><p>Visceral Leishmaniasis, caused by <i>Leishmania donovani,</i> is the second most deadly parasitic disease, causing over 65,000 deaths annually. Synthetic drugs available in the market, to combat this disease, have numerous side effects. In this backdrop, we aim to find safer antileishmanial alternatives with minimal side effects from mushrooms, which harbour various secondary metabolites with promising efficacy. Robust screening of sixteen extracts from eight different wild mushrooms reveals that the hydroalcoholic extract of <i>Amanita princeps</i> has outstanding antileishmanial activity against <i>Leishmania donovani</i>. Metabolomic profiling of this lead extract identifies 50 bioactive mycocompounds and among them, 10 were selected for <i>in-silico</i> study against five major targets-arginase, spermidine synthase, ornithine decarboxylase, trypanothione reductase and SOD, crucial for thiol-redox balance in parasites in the polyamine synthesis pathway. Molecular docking analysis against our prioritised targets identified two mycompounds Ergosterol and Taraxacolide 1-O-b-D-glucopyranoside from <i>Amanita princeps</i> having the highest binding affinity of -15.8 and -11.8 kcal/mol respectively against the ornithine decarboxylase of polyamine synthesis pathway. However, MD simulations and free energy calculation using MM-GBSA analysis revealed the better stability of ergosterol with PASP receptors suggesting its promising role as an anti-leishmanial compound. Further results of in vitro arginase, SOD, and NO enzyme assays also corroborated with <i>in-silico</i> findings, reinforcing the anti-leishmanial efficacy of the <i>Amanita princeps</i> extract. Thus, both in silico and in vitro analyses suggest the efficacy of both Ergosterol and Taraxacolide 1-O-b-D-glucopyranoside compounds resourced from <i>Amanita princeps</i> as potent antileishmanial agents.</p><p><strong>Graphical abstract: </strong></p>","PeriodicalId":94038,"journal":{"name":"In silico pharmacology","volume":"13 1","pages":"6"},"PeriodicalIF":0.0,"publicationDate":"2024-12-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11668711/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142901438","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":"Immunoinformatics-driven design and computational analysis of a multiepitope vaccine targeting uropathogenic <i>Escherichia coli</i>.","authors":"Hina Khalid, Sergey Shityakov","doi":"10.1007/s40203-024-00288-z","DOIUrl":"10.1007/s40203-024-00288-z","url":null,"abstract":"<p><p>Urinary tract infections (UTIs), largely caused by uropathogenic <i>Escherichia coli</i> (UPEC), are increasingly resistant to antibiotics and frequently recur. Using immunoinformatics, we designed a multiepitope peptide vaccine targeting UPEC virulence factors, including iron acquisition systems and adhesins. The construct features 12 cytotoxic T lymphocyte epitopes, six helper T lymphocyte epitopes, and six B-cell epitopes,and isoptimized for high antigenicity, immunogenicity, nontoxic, and low allergenic potential. Molecular docking and 0.4-µs molecular dynamics simulations revealed the molecular mechanism of theinteraction of the vaccine with Toll-like receptor 4 and a favorable binding energy of - 41.83 kcal/mol using an implicit solvation model. These promising in silico results suggest the potential efficacy of the vaccine in preventing UPEC infections and underscore immunoinformatics as a powerful tool for addressing antibiotic-resistant UTI pathogens.</p><p><strong>Graphical abstract: </strong></p><p><strong>Supplementary information: </strong>The online version contains supplementary material available at 10.1007/s40203-024-00288-z.</p>","PeriodicalId":94038,"journal":{"name":"In silico pharmacology","volume":"13 1","pages":"2"},"PeriodicalIF":0.0,"publicationDate":"2024-12-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11663213/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142883681","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":"Virtual screening and molecular dynamics studies of novel small molecules targeting <i>Schistosoma mansoni</i> DHODH: identification of potential inhibitors.","authors":"Saudatu Chinade Ja'afaru, Adamu Uzairu, Vipin Kumar Mishra, Muhammed Sani Sallau, Muhammad Tukur Ibrahim, Amit Dubey","doi":"10.1007/s40203-024-00281-6","DOIUrl":"https://doi.org/10.1007/s40203-024-00281-6","url":null,"abstract":"<p><p>Schistosomiasis affects more than 200 million individuals globally, mainly in underprivileged areas, leading to long-term health issues and adding to socio-economic challenges. The existing reliance on a solitary medication (Praziquantel) gives rise to concerns about drug resistance and possible side effects. The exploration of alternative treatments is crucial to meet the demand for more efficient, safer, and cost-effective remedies, guaranteeing continuous control and eradication initiatives while reducing the risk of drug resistance. To address these issues, we employed a structure-based drug design approach, generating eighteen innovative inhibitors targeting <i>Schistosoma mansoni</i> Dihydroorotate dehydrogenase (SmDHODH). A robust QSAR model yielded promising statistical parameters, and molecular docking of 31 known inhibitors lead to the identification of a lead candidate (Compound <b>21</b>) with favorable binding efficacy. Eighteen novel compounds were designed, showing improved binding affinities compared to both the lead compound and the standard drug, Praziquantel (PZQ). Molecular dynamics simulations and Density Functional Theory (DFT) affirmed the reactivity and stability of protein-ligand complexes under physiological conditions. These compounds exhibit strong inhibition of SmDHODH and meet drug-likeness criteria. Additionally, they demonstrate favorable pharmacokinetic properties, suggesting their potential effectiveness in treating schistosomiasis. Our study underscores the importance of understanding molecular properties for optimizing treatments against this neglected tropical disease.</p><p><strong>Supplementary information: </strong>The online version contains supplementary material available at 10.1007/s40203-024-00281-6.</p>","PeriodicalId":94038,"journal":{"name":"In silico pharmacology","volume":"12 2","pages":"113"},"PeriodicalIF":0.0,"publicationDate":"2024-11-27","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11602894/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142775989","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}