Bioanalysis最新文献

{"title":"Development of an electrochemiluminescence-based bridging assay to detect antibodies against a PTH inverse agonist in human plasma.","authors":"Asvelt J Nduwumwami, Erik J Wagner, Amy Q Wang, Yuhong Fang, Dingyin Tao, Xin Xu","doi":"10.1080/17576180.2026.2709280","DOIUrl":"10.1080/17576180.2026.2709280","url":null,"abstract":"<p><strong>Background: </strong>Therapeutic peptide-induced anti-drug antibodies (ADA) can have various effects, including adverse events and drug-neutralizing activity which can lead to loss of efficacy. This has led regulatory agencies to require nonclinical and clinical testing of biotherapeutics to assess immunogenicity risk.</p><p><strong>Research design and methods: </strong>An electrochemiluminescence bridging assay was developed to detect antibodies against parathyroid hormone receptor inverse agonist (PTH-IA), a novel synthetic peptide that is being developed to treat Jansen's Metaphyseal Chondrodysplasia. Biotinylated PTH-IA and ruthenylated PTH-IA reagents were synthesized via amine-coupling chemistry, and rat polyclonal anti-PTH-IA positive control antibody was generated by immunizing rats with PTH-IA conjugated to keyhole limpet hemocyanin. The reagents were utilized to determine cut points for the screening and confirmatory assays and assay sensitivity in drug-naïve human plasma.</p><p><strong>Results: </strong>Sensitivity of the screening assay was determined to be 3.61 ng/mL at cut point. The cut point for the confirmatory assay was determined to be 9.34% inhibition, and the cut point factor used to establish the floating plate cut point from the negative control signal was 1.055. The assay was found to be selective and reproducible.</p><p><strong>Conclusion: </strong>The assay's performance characteristics demonstrated its suitability for detecting anti-PTH-IA antibodies in human plasma.</p>","PeriodicalId":8797,"journal":{"name":"Bioanalysis","volume":" ","pages":"863-872"},"PeriodicalIF":2.1,"publicationDate":"2026-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13540131/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148700703","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Implementation of cloud-based applications in regulated bioanalytical laboratories - a recommendation from the European Bioanalysis Forum.","authors":"Cecilia Arfvidsson, Harm Buddiger, Werner Schauerte, Katja Zeiser, Lars Ole Andresen, David van Bedaf, Julian Davies, Kristi House, Miroslaw Janowski, Christopher Jones, Rebecca Sleigh, Martina Wein, Elizabeth Wilson-Kruchen, Tony Woodall, Philip Timmerman","doi":"10.1080/17576180.2026.2707045","DOIUrl":"10.1080/17576180.2026.2707045","url":null,"abstract":"<p><p>The adoption of cloud-based applications in regulated bioanalysis has progressed cautiously, largely due to uncertainty regarding the interpretation of existing regulatory expectations and the distribution of responsibilities between organizations and service providers. This recommendation paper from the European Bioanalysis Forum (EBF) provides a bioanalytical perspective on cloud implementation, emphasizing the importance of intended use, data criticality, and cross-functional collaboration throughout the data lifecycle. Rather than prescribing technical solutions, it outlines key considerations for third-party risk management, vendor oversight, and the consistent and proportionate application of existing regulatory principles. Cloud adoption does not change fundamental requirements for data integrity, system validation, or compliance, but introduces a more complex distribution of responsibilities that must be clearly understood and actively managed. The paper supports a risk-based, fit-for-purpose approach that enables confident and effective use of cloud technologies in regulated bioanalysis.</p>","PeriodicalId":8797,"journal":{"name":"Bioanalysis","volume":" ","pages":"853-858"},"PeriodicalIF":2.1,"publicationDate":"2026-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13540121/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148629329","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Highlights from the 17th Japan Bioanalysis Forum Symposium.","authors":"Katsutomo Hata, Naohito Yamada, Hiroyuki Shimizu, Tomoko Arakawa, Hitoshi Uchiyama, Miyuki Ugajin, Takeshi Okuzono, Eiichi Shimada, Masanori Nagata, Masayo Hashimoto, Hisanori Hara, Takashi Miyayama, Tamiki Mori, Ken-Ichi Yamamoto","doi":"10.1080/17576180.2026.2712772","DOIUrl":"10.1080/17576180.2026.2712772","url":null,"abstract":"<p><p>The 17th Japan Bioanalysis Forum Symposium was held in Himeji, Japan, in March 2026. Under the theme \"Unlock Scientific Potential: Future of Bioanalytical Expert,\" the symposium provided a comprehensive forum to share and discuss the latest scientific, technological, and regulatory developments in bioanalysis essential for drug development.The scientific program comprised 12 sessions including 35 oral presentations and 2 panel discussions, 38 general poster presentations, and 12 discussion group poster sessions. The topics spanned a broad range of disciplines, including implementation of ICH M10 and data integrity requirements, bioanalysis of oligonucleotides, gene and cell therapies, antibody-drug conjugates, immunogenicity assessment, biomarker analysis, and advances in LC-MS/MS and ligand‑binding assays. In addition, emerging trends such as artificial intelligence and automation in bioanalytical workflows were actively discussed. The newly introduced sessions for junior bioanalysts and Casual Follow-Up Sessions fostered open dialogue and received particularly strong engagement from the participants. The poster sessions by the individuals and by the discussion groups facilitated lively scientific exchange, further enhanced by the record number of company exhibits. Overall, the symposium successfully highlighted the current challenges and future directions in bioanalysis, reinforcing the critical role of bioanalytical experts in advancing drug development and regulatory science.</p>","PeriodicalId":8797,"journal":{"name":"Bioanalysis","volume":" ","pages":"947-954"},"PeriodicalIF":2.1,"publicationDate":"2026-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13540187/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148705374","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"A validated bioanalytical LC-MS/MS method for the simultaneous determination of molnupiravir, N-hydroxycytidine, and baricitinib in human plasma.","authors":"Fatma H Ghazy, Ramzia I El-Bagary, Samar H Fahim, Sally T Mahmoud","doi":"10.1080/17576180.2026.2715920","DOIUrl":"10.1080/17576180.2026.2715920","url":null,"abstract":"<p><p>A sensitive and validated liquid chromatography-tandem mass spectrometry (LC-MS/MS) method was developed for the simultaneous quantification of the anti-COVID-19 agents molnupiravir (MPV), its active metabolite N-hydroxycytidine (NHC), and baricitinib (BARI) in human plasma. As MPV is rapidly converted to NHC <i>in vivo</i>, whereas BARI is predominantly eliminated unchanged, NHC was generated <i>in vitro</i> by alkaline hydrolysis to enable accurate determination of the active metabolite. Chromatographic separation was achieved on an Agilent Poroshell 120 EC-C18 column using methanol and 0.1% formic acid in water (90:10, v/v). Escitalopram was selected as the internal standard owing to its consistent extraction recovery, and satisfactory chromatographic performance. Plasma samples were prepared by liquid-liquid extraction with ethyl acetate, yielding recoveries of 87.5-91.6% for MPV, 87.5-89.4% for NHC, and 87.9-94.9% for BARI. The method was validated according to FDA bioanalytical guidelines over concentration ranges of 20-500, 20-10.000, and 20-500 ng/mL for MPV, NHC, and BARI, respectively. Accuracy, precision, stability, recovery, carryover, and matrix effect met the acceptance criteria. Normalized matrix factors for MPV, NHC, and BARI ranged from 0.948-0.984, 0.900-0.902, and 0.912-1.014, respectively, with CV values below 1%, indicating negligible matrix interference. The proposed method provides a reliable analytical tool for future pharmacokinetic and therapeutic drug monitoring studies.</p>","PeriodicalId":8797,"journal":{"name":"Bioanalysis","volume":" ","pages":"1015-1029"},"PeriodicalIF":2.1,"publicationDate":"2026-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13540238/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148763979","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Dry chemistry-based approaches for point-of-care (POC) diagnostics.","authors":"Tanmayee Deshpande, Oyessi Dutta, Akshay Parmar, Marimuthu Citartan, Naresh Kumar Mani","doi":"10.1080/17576180.2026.2701601","DOIUrl":"10.1080/17576180.2026.2701601","url":null,"abstract":"<p><p>In the field of diagnosis, where minimal costs, less processing time, low labor, and high accuracy are critical aspects, the integration of dry chemistry principles with microfluidic approaches has led to a significant streamlining of procedures in the field. The literature for this review was collected from databases such as Google Scholar and PubMed, primarily covering studies published between 2020 and 2025. Dry chemistry is an evolving branch of analytical chemistry that uses primarily dry or immobilized reagents, enabling rapid and reliable analysis without extensive sample preparation. This paper extensively examines the principles and methods of detecting the prominent biomarkers of the biological samples used in diagnosis. It also provides a comparative analysis of conventional diagnostic techniques focused on wet chemistry principles and dry chemistry-based methods, further highlighting the efficient selectivity and broader applicability in diverse clinical settings. This study also focuses on the commercialization of dry chemistry analyzers. It further elaborates on the increasing market share, ongoing advancements in technology, and relevance of point-of-care devices in limited resource-based clinical settings, where accessibility, portability, and reliability are a few of the challenging issues.</p>","PeriodicalId":8797,"journal":{"name":"Bioanalysis","volume":" ","pages":"911-932"},"PeriodicalIF":2.1,"publicationDate":"2026-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13540120/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148598230","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Vaccine Ligand Binding Assay Development.","authors":"Thorsten Verch, Luc Gagnon, Alessandra Buoninfante, Leslie Wagner, Meenu Wadhwa, Chad Irwin, Christian Mayer, João Tavares Neto, Joseph Agnes, Anastasia Aksyuk, Angelique Baclin, Marie Bonhomme, Shane Cloney-Clark, Bart Corsaro, Francis Dessy, Louis Fries, Fabio Garofolo, Peter Giardina, Tina Green, Nuria Guimera, Shannon Harris, Roy Helmy, James Huleatt, Akiko Ishii-Watabe, Ralf Jaeger, Dewal Jani, Sarah Janssen, Julie Joseph, Lisa Kierstead, Karen Makar, Jean-Claude Marshall, Dulcyane Neiva Mendes, Rocio Murphy, Sankeetha Nadarajah, Katrina Nolan, Joyce Plested, Ingrid Scully, Ivo Sonderegger, Jeroen Stoop, Charles Tan, Deidre Wilkins, Arron Xu, Lingyi Zheng, Mingzhu Zhu","doi":"10.1080/17576180.2026.2708544","DOIUrl":"10.1080/17576180.2026.2708544","url":null,"abstract":"<p><p>This white paper (Part 2 of a series on vaccine immunogenicity assay validation) addresses the development of Ligand Binding Assays (LBAs) to support vaccine immunogenicity studies. Developed through a collaborative effort by a working group of experts from 16 global vaccine manufacturers, national regulatory authorities, and a nonprofit global-health foundation convened under the Workshop on Recent Issues in Bioanalysis (WRIB), this manuscript provides practical guidance to complement existing regulatory frameworks for bioanalytical method validation.Part 2 details the iterative process of LBA development, with emphasis on defining the Analytical Target Profile (ATP) as a foundational tool for guiding decision-making across the assay life cycle. Key topics include assay purpose and analyte specificity, regulatory expectations, the use of statistical Design of Experiments (DOE) to systematically optimize assay conditions, and the selection of appropriate reagents, controls, and sample matrices. The paper also addresses the unique challenges posed by the structural diversity of vaccine antigens and the need for representative reference materials.The manuscript further highlights the importance of ongoing performance assessment and the adaptability of assays as they transition from early exploratory phases to pivotal clinical studies. Collectively, the recommendations presented aim to supplement existing regulatory guidance with vaccine-specific considerations, ultimately supporting the development of safe and effective vaccines. This paper is complemented by Part 1 (LBA Validation) and Part 3 (Assay Lifecycle Management, including Maintenance, Monitoring, and Transfers).</p>","PeriodicalId":8797,"journal":{"name":"Bioanalysis","volume":" ","pages":"839-851"},"PeriodicalIF":2.1,"publicationDate":"2026-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13540139/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148787656","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Electrochemiluminescence immunoassay for quantifying ZMA001 in human serum: method development, validation, and clinical pharmacokinetic application.","authors":"Abdul-Azeez A Lanihun, Oluwatobi T Arisa, Olivia Poczatek, Yi Zeng, Nam Hoon Kwon, Sunghoon Kim, Sandra Cooper, Jason M Elinoff, William D Figg","doi":"10.1080/17576180.2026.2715919","DOIUrl":"10.1080/17576180.2026.2715919","url":null,"abstract":"<p><p>ZMA001 is a novel human IgG1 monoclonal antibody (mAb) specifically designed to target the N-terminal region of transmembrane lysyl-tRNA synthetase 1 (KARS1), an enzyme implicated in the pathobiology of pulmonary arterial hypertension. The study aimed to develop a bioanalytical method to quantify ZMA001 in human sera to support a phase 1 clinical trial (NCT05967299). An indirect Electrochemiluminescence Immunoassay (ECLIA) method was developed employing KARS1 antigen as the capture reagent and SULFOTAG goat antihuman antibody as the secondary antibody. The method was subsequently validated in accordance with relevant guidelines, including those of the International Council for Harmonization (ICH). The assay's quantification range was established at 0.5-50 µg/mL. The assay was accurate, precise, and selective for the determination of ZMA001 concentrations in human serum. Results revealed that ZMA001 was stable at room temperature for over 4 hours and could withstand multiple freeze-thaw cycles. No prozone/hook effect was apparent in the assay range. Based on preliminary pharmacokinetic data, the average maximum concentration is 41.8 μg/mL while the half-life is about 9.9 days. The method provides a rapid and sensitive approach for the quantitative assessment of ZMA001 in human serum and is well-suited for use in ongoing and future clinical studies.</p>","PeriodicalId":8797,"journal":{"name":"Bioanalysis","volume":" ","pages":"961-969"},"PeriodicalIF":2.1,"publicationDate":"2026-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13540125/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148711245","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Comparison of TISAB II and III for salivary fluoride determination: addressing a bioanalytical challenge in fluoride analysis.","authors":"Flavia Almeida Amorim, Maria Suzi de Sousa Lopes, Lyzia Vitoria Mendes Rezende, Evanildo Canuto Paz, Marcus Vinícius Oliveira, Glauber Campos Vale","doi":"10.1080/17576180.2026.2712771","DOIUrl":"10.1080/17576180.2026.2712771","url":null,"abstract":"<p><strong>Background: </strong>Accurate determination of salivary fluoride (F) depends on appropriate analytical conditions, particularly the buffering system used before ion-selective electrode measurements.</p><p><strong>Research design and methods: </strong>This laboratory-based analytical study addressed the practical challenge of selecting between two total ionic strength adjustment buffers (TISAB II and TISAB III) for salivary F-determination using samples obtained from previously conducted clinical trials. Unstimulated saliva from eight participants was collected at baseline and at 5 min, 30 min, 1 h, 4 h, and 12 h after exposure to three F-treatments: F-varnish, 1,450 ppm F-dentifrice, and 5,000 ppm F-dentifrice. F-concentrations were measured using an F-ion-selective electrode after buffering with either TISAB II or TISAB III. Data were analyzed using paired statistical tests and Pearson correlation analysis (α = 0.05).</p><p><strong>Results: </strong>No significant differences were observed between the buffers across most conditions, although differences were detected at later time points following dentifrice use. A strong positive correlation was found between the two buffering systems (<i>p</i> < 0.001), and no differences were detected in the area under the concentration-time curve.</p><p><strong>Conclusions: </strong>These findings indicate that both TISAB II and TISAB III provide comparable analytical performance for salivary fluoride determination under the tested conditions, although differences may occur at lower fluoride concentrations.</p>","PeriodicalId":8797,"journal":{"name":"Bioanalysis","volume":" ","pages":"955-960"},"PeriodicalIF":2.1,"publicationDate":"2026-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13540148/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148652828","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"From anti-drug antibody incidence to clinical relevance: interpreting highly sensitive immunogenicity assays in biosimilars.","authors":"Anita Krishnan, Somesh Bp, Gaurav Mehta, Shilpa Ramaswamy, Soumen Chakraborty, Shyamapada Mandal","doi":"10.1080/17576180.2026.2715917","DOIUrl":"10.1080/17576180.2026.2715917","url":null,"abstract":"<p><strong>Background: </strong>Highly sensitive anti-drug antibody (ADA) assays in biosimilar comparative trials can generate high apparent positivity clustered near decision thresholds without corresponding clinical impact. Using approved biosimilars of ustekinumab and denosumab, this work retrospectively examines alternate analytical strategies to improve the biological interpretability of ADA findings.</p><p><strong>Methods: </strong>Clinical ADA datasets were re-analyzed using a variability-anchored minimum screening cut point (mSCP), magnitude-aware log S/N versus percent inhibition contour visualization, and subject-level classification into preexisting, treatment-boosted, and treatment-emergent categories. A subset of the data was also subjected to longitudinal change from baseline evaluation.</p><p><strong>Results: </strong>Conventional tiered analysis produced overall screening sample positivity of 48-82% across all studies and subject-level ADA incidence >80% in 10 of the 11 arms (range, 64-100%), without any corresponding impact on pharmacokinetics, safety, or efficacy. The mSCP-based approach reduced cut point-adjacent noise-consistent signals, enabling subject-level classification that is clinically more relevant. Longitudinal analysis further separated persistent from transient responses.</p><p><strong>Conclusion: </strong>Biosimilar immunogenicity testing is a confirmatory exercise against an already-approved reference, not an investigative characterization. As regulatory frameworks move toward reduced reliance on comparative Phase 3 studies, identifying persistent ADA responses at Phase 1 becomes increasingly important; a fit-for-purpose, comparability-anchored analytical strategy warrants collective regulatory rethinking.<b>Clinical trial registration:</b> www.isrctn.com; identifier: ISRCTN1142400EudraCT Number: 2021-006668-25;ClinicalTrials.gov: NCT05335356 ClinicalTrials.gov: NCT05323708EudraCT number: 2021-006545-36, CT.gov number: NCT05345691.</p>","PeriodicalId":8797,"journal":{"name":"Bioanalysis","volume":" ","pages":"1001-1014"},"PeriodicalIF":2.1,"publicationDate":"2026-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13540081/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148817333","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Advancing beyond stand-alone NAb assays: perspectives and regulatory impact of applying integrated immunogenicity assessment in drug development.","authors":"Kirstee Martin, Marit Lichtfuss, Devangi Mehta","doi":"10.1080/17576180.2026.2690264","DOIUrl":"10.1080/17576180.2026.2690264","url":null,"abstract":"<p><p>Neutralizing antibody (NAb) activity assessment is a regulatory expectation in the clinical development of therapeutic proteins, traditionally addressed through standalone NAb assays. However, evolving regulatory guidance and industry experience increasingly recognize that integrated analyses of anti-drug antibodies (ADA), pharmacokinetics (PK), pharmacodynamics (PD), efficacy, and safety may provide a more clinically meaningful evaluation of neutralizing activity. This perspective examines the scientific and regulatory rationale for moving beyond routine reliance on standalone NAb assays and describes a risk-based, integrated immunogenicity assessment framework. Two case studies involving low-risk monoclonal antibodies-garadacimab and clazakizumab-are presented, in which validated standalone NAb assays were available but not relied upon for primary clinical interpretation due to limited sensitivity and lack of added clinical value. Instead, longitudinal ADA characterization integrated with PK and PD or efficacy data was used to assess clinically meaningful neutralizing activity. In both cases, this approach enabled clear differentiation between detectable but clinically irrelevant immunogenicity and immunogenicity with clinical consequence and was accepted by regulatory authorities. These examples illustrate how integrated immunogenicity assessments can replace standalone NAb assays while remaining scientifically rigorous, clinically informative, and aligned with regulatory expectations.</p>","PeriodicalId":8797,"journal":{"name":"Bioanalysis","volume":" ","pages":"797-805"},"PeriodicalIF":2.1,"publicationDate":"2026-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC13557571/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"148315572","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}