ADMET and DMPK最新文献

{"title":"Engineering affibody-based biosensing platforms for cancer biomarker detection.","authors":"Zhafira Fauziah, Robeth Viktoria Manurung, Yuspian Nur, Dika Apriliana Wulandari, Salma Nur Zakiyyah, Irkham, Yeni Wahyuni Hartati","doi":"10.5599/admet.3363","DOIUrl":"10.5599/admet.3363","url":null,"abstract":"<p><strong>Background and purpose: </strong>Cancer is one of the most life-threatening diseases and has the highest mortality rate worldwide. Delayed cancer diagnosis remains a major challenge in cancer treatment. Currently, conventional diagnostic methods still have several limitations, resulting in many cancer cases being detected only at advanced stages.</p><p><strong>Experimental approach: </strong>This review was conducted as a literature study of research on the development of affibody-based biosensors for cancer biomarker detection. The review discusses the characteristics of affibodies as bioreceptors, affibody synthesis methods, and their applications in electrochemical and optical biosensors.</p><p><strong>Key results: </strong>Various studies have shown that affibody-based biosensors exhibit high sensitivity and specificity for detecting cancer biomarkers such as human epidermal growth factor receptor 2, tumour necrosis factor-alpha, epidermal growth factor receptor, carcinoembryonic antigen and alpha-fetoprotein. The integration of affibodies into biosensor platforms enables low detection limits, wide linear ranges and good analytical performance in biological samples.</p><p><strong>Conclusion: </strong>Affibody-based biosensors show great potential as platforms for cancer diagnosis. The use of affibodies as bioreceptors offers several advantages over antibodies and aptamers, particularly ease of synthesis, high stability and strong binding affinity.</p>","PeriodicalId":7259,"journal":{"name":"ADMET and DMPK","volume":"14 ","pages":"3363"},"PeriodicalIF":5.1,"publicationDate":"2026-06-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13499663/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148786905","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 antitubercular evaluation of novel 5,6-diphenyl-1,2,4-triazine-piperazine derivatives targeting mycobacterial dihydrofolate reductase.","authors":"Uday Thakkar, Moksh Shah, Pratik Khona, Harnisha Patel, Mange Ram Yadav, Salman Patel, Chanchal Singh, Renuka Bhamre, Afzal Nagani","doi":"10.5599/admet.3322","DOIUrl":"10.5599/admet.3322","url":null,"abstract":"<p><strong>Background and purpose: </strong>Tuberculosis (TB), a serious global health concern, continues to contribute to the global health burden, underscoring the urgent need to discover potent antitubercular agents. In the present study, a series of novel 5,6-diphenyl-1,2,4-triazine-piperazine derivatives were synthesized, and their potential for anti-tubercular activity was assessed.</p><p><strong>Experimental approach: </strong>The antitubercular potential of the synthesized compounds was assessed using the microplate alamar blue assay (MABA). Cytotoxicity studies were carried out on RAW 264.7 macrophages. To assess the mode of action of the synthesized compounds, docking analysis of the active compounds was performed on two key enzymes of <i>Mycobacterium</i>, decaprenylphosphoryl-β-D-ribose 2'-epimerase and <i>Mycobacterium tuberculosis</i>-dihydrofolate reductase (<i>Mtb</i>-DHFR). Furthermore, molecular dynamics simulations and density functional theory calculations were performed to validate the stability of the ligand-protein complexes and the electronic properties of the lead compounds.</p><p><strong>Key results: </strong>The results revealed promising anti-tubercular activity for the synthesized compounds. Among these, compounds 2-((5,6-Diphenyl-1,2,4-triazin-3-yl)thio)--1-(4-(4-fluorobenzoyl)piperazin-1-yl)ethan-1-one (FP3) and 2-((5,6-diphenyl-1,2,4-triazin-3-yl)thio)-1-(4-(4-methylbenzoyl) piperazin--1-yl)ethan-1-one (FP8) exhibited potent activity with an minimum inhibitory concentration of 1.6 μg mL^-1, along with promising cytotoxicity profiles against RAW 264.7 macrophage cells. Docking studies revealed potent docking scores compared to the standard, thereby confirming the involvement of the DHFR enzyme. Interaction analysis revealed stable hydrogen-bond interactions, π-π stacking, and hydrophobic interactions with the active-site residues of the DHFR enzyme. Additionally, molecular dynamics simulation validated the stability of the interactions and the structural integrity of the complexes, while density functional theory calculations supported the desirable electronic properties of the lead compounds.</p><p><strong>Conclusion: </strong>The combined results of the experiments and calculations validated the potential of FP3 and FP8 as DHFR-targeted antitubercular agents. The study highlights the potential of 5,6-diphenyl-1,2,4-triazine-piperazine derivatives as promising candidates for further anti-tubercular drug development.</p>","PeriodicalId":7259,"journal":{"name":"ADMET and DMPK","volume":"14 ","pages":"3322"},"PeriodicalIF":5.1,"publicationDate":"2026-06-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13499672/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148786848","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 characterization of bimetallic nanocomplex: Application for electrochemical determination of idarubicin as anti-cancer drug.","authors":"Thekrayat Joodi Jassim, Raheem Kubaish Barid, Haider Dakhal Hamza","doi":"10.5599/admet.3342","DOIUrl":"10.5599/admet.3342","url":null,"abstract":"<p><strong>Background and purpose: </strong>Cancer chemotherapy with antineoplastic drugs destroys cancer cells through complete cell death or stops cell development while protecting healthy cells from damage. Monitoring anticancer therapeutics in blood and tissues is important for determining their fate.</p><p><strong>Experimental approach: </strong>A novel binuclear complex with the formula [Cu(opd)₂(H₂O)(μ-SCN)Ni(opd)(SCN)₃] (opd = o-phenylenediamine) was synthesized and characterized using Fourier transform infrared spectroscopy and UV-Vis spectroscopy. The solvothermal method was used to create a nanoscale version of the binuclear complex. X-ray powder diffraction, scanning electron microscopy, UV-Vis and FT-IR spectroscopy were used to characterize the nanocomplex. The solvothermal approach produced a nanocomplex with an average size of around 56 nm. The complex was tested for its antimicrobial properties on Gram-positive <i>Staphylococcus aureus</i> and <i>Enterococcus faecalis</i>, as well as Gram-negative <i>Escherichia coli</i> and <i>Pseudomonas aeruginosa</i>. Additionally, a screen-printed graphite electrode modified by a synthetic nanocomplex (Cu-Ni/SPGE) was presented as an improved electrochemical sensor for the detection of idarubicin (IRN).</p><p><strong>Key results: </strong>This sensor has a linear dynamic range from 0.01 to 3.0 μM and an impressive limit of detection of 0.003 μM under ideal testing circumstances.</p><p><strong>Conclusion: </strong>The researchers used a Cu-Ni/SPGE system to perform electrochemical measurements on IRN. The Cu-Ni/SPGE outperformed the untreated SPGE in terms of IRN oxidation. The antibacterial activity of the complex was also studied.</p>","PeriodicalId":7259,"journal":{"name":"ADMET and DMPK","volume":"14 ","pages":"3342"},"PeriodicalIF":5.1,"publicationDate":"2026-06-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13499671/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148786930","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":"Enhanced anti-inflammatory and antibacterial efficacy of a novel gum ghatti-infused polymeric film for ocular drug delivery.","authors":"Swagatika Das, Sk Habibullah, Yashwant Giri, Amulyaratna Behera, Gurudutta Pattnaik, Biswaranjan Mohanty","doi":"10.5599/admet.3200","DOIUrl":"10.5599/admet.3200","url":null,"abstract":"<p><strong>Background and purpose: </strong>Ocular inflammation is a key challenge after ocular surgery, and resistance has developed in the bacterial strain. Primarily, the short residence time of the ocular formulation makes it more effective in treating and alleviating inflammation.</p><p><strong>Experimental approach: </strong>In this study, a moxifloxacin-incorporated gum ghatti-infused poly(vinyl alcohol-chitosan) polymeric film was developed by solvent casting. Various properties of the ocular composite film, including mucoadhesiveness, strength profile, and crystal size, were evaluated.</p><p><strong>Key results: </strong>The prepared composite film exhibited a red-yellow hue. XRD and DSC analyses revealed that the drug in the formulation is amorphous. The release profile reduces the release rate and follows both Fickian- and non-Fickian-mediated pathways. A clear zone of inhibition was observed against both Gram-negative (<i>Pseudomonas aeruginosa</i>) and Gram-positive (<i>Staphylococcus aureus</i>) bacteria. The in vivo anti-inflammatory potential of carrageenan was observed against the prepared formulations, and within 1.5 hours, redness and inflammation diminished. Corneal integrity was maintained, with no dark spots observed in the corneal region, confirming that no coagulant or thrombosis of blood occurred in the eye.</p><p><strong>Conclusion: </strong>Based on the foregoing discussion, the formulation shows potential for treating ocular conjunctivitis and can be safely used for pink eye, bacterial conjunctivitis, or allergic conjunctivitis.</p>","PeriodicalId":7259,"journal":{"name":"ADMET and DMPK","volume":"14 ","pages":"3200"},"PeriodicalIF":5.1,"publicationDate":"2026-05-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13499658/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148786862","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":"Assessing oxime reactivation efficacy using principal component analysis: Insights from nerve agents inhibited human butyrylcholinesterase.","authors":"Goran Šinko, Tena Čadež, Zrinka Kovarik, Nikolina Maček Hrvat","doi":"10.5599/admet.3361","DOIUrl":"10.5599/admet.3361","url":null,"abstract":"<p><strong>Background and purpose: </strong>The toxicity of organophosphorus compounds (OPs) and related nerve agents (NAs) impairs the cholinergic system via irreversible inhibition of acetylcholinesterase (AChE) activity by phosphylation of the catalytic serine. Reactivation of the enzyme activity largely depends on the structural compatibility between the enzyme, an oxime reactivator, and the specific OP compound.</p><p><strong>Experimental approach: </strong>For this study, we used our recently published data on the reactivation of human butyrylcholinesterase inhibited by the NAs sarin, cyclosarin, tabun and VX, using a library of 115 oximes. We compared these results with oximes' ADME (absorption, distribution, metabolism, and excretion) parameters relevant to central nervous system activity using principal component analysis (PCA). PCA facilitated the examination of these relatively large datasets by increasing interpretability while minimizing information loss.</p><p><strong>Key results: </strong>Three components with eigenvalues above 1 resulted in 72 % of the cumulative proportion of variance and described 27 variables. PC1 created transformed data that had negative values for most oximes with high reactivation potential, while showing large positive values for oximes with moderate and low efficacy. Distribution of 27 loadings, representing 27 variables, produced a set of 9 positive and 18 negative loadings representing negative and positive data correlation. The efficacy of oxime reactivation was highly correlated with the parameters describing its structure: molecular weight, rotational bonds, molecular volume, and molecular surface area.</p><p><strong>Conclusion: </strong>A large dataset was efficiently analysed by maximizing the preservation of variability and generating new, uncorrelated variables. To our knowledge, this study is the first to apply PCA to assess oxime's reactivation efficacy, thus providing insights into the relationships between oxime properties and their efficacy in restoring OP-inhibited cholinesterase activity.</p>","PeriodicalId":7259,"journal":{"name":"ADMET and DMPK","volume":"14 ","pages":"3361"},"PeriodicalIF":5.1,"publicationDate":"2026-05-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13499654/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148786842","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":"Magnetoreceptive CRY/MagR complexes: linking circadian redox signalling to protein aggregation in Alzheimer's and Parkinson's disease.","authors":"Mozhgan Alipour, Behnam Hajipour-Verdom, Faria Ashrafi, Sara Rahmati Roodsari, Shabnam Nohesara, Alireza Zali, Farzad Ashrafi","doi":"10.5599/admet.3366","DOIUrl":"10.5599/admet.3366","url":null,"abstract":"<p><strong>Background and purpose: </strong>Neurodegenerative disorders such as Alzheimer's disease (AD) and Parkinson's disease (PD) pose an escalating challenge to neuroscience, as disease-modifying therapies remain elusive despite substantial advances in molecular and cellular understanding. These disorders share convergent pathological features, including protein misfolding and aggregation, mitochondrial dysfunction, oxidative stress, impaired proteostasis, and disruption of circadian regulation. Identifying integrative frameworks that connect these processes is therefore essential for advancing conceptual models of neurodegeneration. This review examines magneto-proteins, with a particular focus on CRY/MagR-based magnetoreceptor complexes, as emerging biological systems that may intersect with key molecular pathways implicated in AD and PD.</p><p><strong>Experimental approach: </strong>We synthesized literature from neuroscience, biophysics, and circadian biology to evaluate the potential relevance of magnetoreceptor mechanisms to AD and PD pathology. We first summarized the core neuropathological mechanisms underlying both diseases, including amyloid-β and tau pathology in AD and α-synuclein aggregation and dopaminergic vulnerability in PD. We then outlined the biophysical foundations of magneto-protein function, emphasizing cryptochrome-mediated radical pair mechanisms, iron-sulphur cluster-dependent magnetic sensitivity, and their established roles in redox signalling and circadian biology.</p><p><strong>Key results: </strong>Accumulating experimental evidence from cellular and animal models suggests that CRY/MagR-associated pathways can modulate oxidative stress, mitochondrial bioenergetics, protein aggregation dynamics, autophagic processes, and circadian control of neuronal metabolism. These processes closely overlap with molecular determinants of neuronal vulnerability in AD and PD. However, direct validation in mammalian and human systems remains limited and controversial, representing a critical knowledge gap.</p><p><strong>Conclusion: </strong>The mechanistic convergence between magnetoreceptor biology and neurodegenerative pathology warrants critical evaluation but remains largely speculative in humans. By integrating findings across disciplines, this review positions CRY/MagR-based magneto-proteins as a conceptual platform for exploring how magnetic field-responsive molecular systems may inform our understanding of neurodegenerative disease mechanisms, while emphasizing the need for rigorous mammalian validation.</p>","PeriodicalId":7259,"journal":{"name":"ADMET and DMPK","volume":"14 ","pages":"3366"},"PeriodicalIF":5.1,"publicationDate":"2026-05-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13499655/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148786858","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-activity relationship of captopril derivatives as New Delhi metallo beta-lactamase 1 inhibitors.","authors":"Ikhlas Jarrar","doi":"10.5599/admet.3304","DOIUrl":"10.5599/admet.3304","url":null,"abstract":"<p><strong>Background and purpose: </strong>New Delhi Metallo beta-lactamase-1 (NDM-1) is a zinc-dependent enzyme that confers resistance to several antibiotics; therefore, there is an urgent requirement for effective inhibitors. Captopril has been exploited as a scaffold in the design of NDM-1 inhibitors; however, a comparative evaluation of these derivatives from structure activity relationship perspective has not been conducted. This review aimed to evaluate captopril-derived NDM-1 inhibitors and to identify possible structure-activity relationships that govern their NDM-1 inhibitory action.</p><p><strong>Experimental approach: </strong>The literature was searched in a structured manner using scholarly databases to locate original studies that reported captopril derivatives and evaluated them in vitro against NDM-1 with the explicit reporting of the inhibitory concentration values (IC₅₀). Eligible studies were filtered using predefined criteria and analysed using a qualitative approach, because heterogeneity in assay conditions and experimental methods prevented a direct quantitative comparison across studies.</p><p><strong>Important findings: </strong>The activity of captopril derivatives depends on the free thiol group (masking it reduces activity), with stereochemistry governing optimal binding orientation within the NDM-1 active site, hydrophobic substitutions enhance activity only within steric limits, and the carboxylate motif serves as a secondary anchoring feature.</p><p><strong>Conclusion: </strong>Captopril emerges as a promising scaffold for NDM-1 inhibitors and reveals significant structural features associated with NDM-1 inhibitors. Despite limited in vivo data and heterogeneity in assay conditions, the findings provide a rational framework for optimizing captopril-inspired NDM-1 inhibitors.</p>","PeriodicalId":7259,"journal":{"name":"ADMET and DMPK","volume":"14 ","pages":"3304"},"PeriodicalIF":5.1,"publicationDate":"2026-05-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13499674/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148786875","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":"Prediction of bile salt export pump inhibition using biomimetic chromatographic descriptors: Integrating membrane affinity and protein binding.","authors":"Chrysanthos Stergiopoulos, Klara Valko","doi":"10.5599/admet.3303","DOIUrl":"10.5599/admet.3303","url":null,"abstract":"<p><strong>Background and purpose: </strong>Bile salt export pump (BSEP) inhibition is a key mechanistic driver of cholestatic drug-induced liver injury, yet current prediction approaches rely mainly on in vitro potency and calculated physicochemical descriptors that do not adequately reflect local exposure at the canalicular membrane. This study aimed to evaluate whether biomimetic chromatographic descriptors could improve predictions of BSEP inhibition by incorporating mechanistically relevant information on membrane affinity and protein binding.</p><p><strong>Experimental approach: </strong>A dataset of 62 structurally diverse compounds with reported BSEP inhibition data was compiled and modelled using multiple linear regression. Biomimetic descriptors derived from immobilized artificial membrane chromatography and human serum albumin affinity (log <i>k</i> _HSA) were compared against conventional descriptors such as lipophilicity and molecular weight. Model performance was assessed using internal and external validation, graphical diagnostics, Y-randomization, and applicability domain analysis.</p><p><strong>Key results: </strong>Models based on biomimetic descriptors demonstrated superior, more balanced predictive performance than conventional physicochemical models, with greater robustness and external predictivity. The combination of membrane-affinity and protein-binding descriptors provided a more accurate representation of the determinants governing BSEP interactions.</p><p><strong>Conclusion: </strong>Biomimetic chromatographic descriptors provide an experimentally grounded approximation of membrane-proximal exposure, a key determinant of BSEP interactions that conventional descriptors do not capture. This approach extends beyond traditional quantitative structure-activity relationship by incorporating distribution-relevant properties into predictive modelling and offers a simple, interpretable framework to support early identification of transporter-mediated toxicity risk in drug discovery.</p>","PeriodicalId":7259,"journal":{"name":"ADMET and DMPK","volume":"14 ","pages":"3303"},"PeriodicalIF":5.1,"publicationDate":"2026-05-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13499664/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148786933","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 of NiO nanostructures as electrode materials for the voltammetric determination of epinephrine in the presence of acetaminophen.","authors":"Mais A Mohammed, Shemaa A Soud, Reem Adham Al-Bayati, Shimaa B Al-Baghdadi","doi":"10.5599/admet.3201","DOIUrl":"10.5599/admet.3201","url":null,"abstract":"<p><strong>Background and purpose: </strong>Epinephrine, also called noradrenaline, is an important chemical mediator in the central nervous system of mammals.</p><p><strong>Experimental approach: </strong>The hydrothermally synthesized NiO nanostructures were used for the modification of a screen-printed electrode, and they were characterized and used in this work for the voltammetric determination of epinephrine in the presence of acetaminophen. Several electrochemical techniques were employed to investigate the electrochemical properties of NiO-modified screen-printed carbon electrode, including cyclic voltammetry, differential pulse voltammetry and chronoamperometry.</p><p><strong>Key results: </strong>The differential pulse voltammetry peak current of epinephrine was linear with concentration in the range from 0.01 to 400.0 μmol L^-1, and the limit of detection was 0.005 μM with a sensitivity of 0.1167 μA L μmol^-1. The findings indicated that the current signals for epinephrine were significantly amplified, a result attributed to the superior catalytic performance of the NiO nanostructures. Furthermore, the oxidation peaks for epinephrine and acetaminophen were distinctly separated, with potential differences of approximately 360 mV and 545 mV, respectively.</p><p><strong>Conclusion: </strong>Furthermore, the NiO modified screen-printed carbon electrode was successfully applied to quantify epinephrine and acetaminophen in both urine samples and pharmaceutical formulations. The results indicated satisfactory recovery rates for the target analytes. Consequently, this electrode is suitable for the analysis of both compounds in pharmaceutical and clinical laboratory settings.</p>","PeriodicalId":7259,"journal":{"name":"ADMET and DMPK","volume":"14 ","pages":"3201"},"PeriodicalIF":5.1,"publicationDate":"2026-05-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13499668/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148786840","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":"Leveraging network pharmacology in the treatment of asthma.","authors":"Sarthi Ahuja, Richard C Kashindye, Divya Yadav, Priyanka Chaudhary, Rakesh Yadav","doi":"10.5599/admet.3281","DOIUrl":"10.5599/admet.3281","url":null,"abstract":"<p><strong>Background and purpose: </strong>Asthma, a chronic airway inflammatory disorder driven by multifaceted genetic, cellular and molecular interactions, remains inadequately managed by single-target therapies due to incomplete disease control and adverse effects; this review aimed to explore network pharmacology's role in elucidating multi-target mechanisms of phytotherapeutic agents for asthma, with a focus on integrating ADMET/DMPK profiling to predict clinical translatability and safety.</p><p><strong>Experimental approach: </strong>We employed network pharmacology methodologies including target prediction (<i>e.g. via</i> PharmMapper, PubChem), protein-protein interaction network construction (STRING, Cytoscape), pathway enrichment analysis (KEGG, Reactome), molecular docking (AutoDock) and ADMET/DMPK modelling (SwissADME, pkCSM) to dissect multi-component herbal formulations, complemented by literature-mined experimental validations.</p><p><strong>Key results: </strong>Analyses identified key asthma-related targets (<i>e.g.</i> IL-17, TNF) and pathways (JAK-STAT, PI3K-AKT), revealing quercetin and kaempferol's multi-target efficacy in reducing airway inflammation and immune dysregulation; favourable ADMET profiles (high oral bioavailability, low toxicity) and DMPK parameters (metabolic stability <i>via</i> CYP inhibition) supported their therapeutic potential in herbal combinations.</p><p><strong>Conclusion: </strong>Network pharmacology, enhanced by ADMET/DMPK integration, advances a holistic understanding of herbal asthma treatments, promoting safe, multi-target drug development. Limitations include data gaps in multi-omics validation and herbal standardization, with future directions leveraging AI-driven predictions for personalized pharmacotherapy.</p>","PeriodicalId":7259,"journal":{"name":"ADMET and DMPK","volume":"14 ","pages":"3281"},"PeriodicalIF":5.1,"publicationDate":"2026-05-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13499659/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148786888","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}