{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,3,27]],"date-time":"2026-03-27T14:52:09Z","timestamp":1774623129758,"version":"3.50.1"},"reference-count":46,"publisher":"Wiley","issue":"5","license":[{"start":{"date-parts":[[2026,2,12]],"date-time":"2026-02-12T00:00:00Z","timestamp":1770854400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"},{"start":{"date-parts":[[2026,2,12]],"date-time":"2026-02-12T00:00:00Z","timestamp":1770854400000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/doi.wiley.com\/10.1002\/tdm_license_1.1"}],"content-domain":{"domain":["onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["Small Methods"],"published-print":{"date-parts":[[2026,3]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n                  <jats:p>The interfacial stability of therapeutic monoclonal antibodies (mAbs) remains a critical challenge in pharmaceutical development, particularly in the context of biocompatible silicone oil\u2010coated delivery devices. Here, we present a molecular\u2010level investigation of antibody conformational dynamics at model polydimethylsiloxane (PDMS) interfaces under varying pH conditions. Using a multi\u2010technique approach combining neutron reflection (NR), spectroscopic ellipsometry (SE), and quartz crystal microbalance with dissipation (QCM\u2010D), the pH\u2010dependent structural adaptations of two engineered antibodies, COE\u20103 and COE\u20107, and their constituent Fab and Fc fragments were revealed. Both COE\u20103 and COE\u20107 underwent distinct conformational transitions between pH 5.5 and 8.0, with a remarkable shift from monolayer to bilayer architectures. At pH 5.5, both antibodies formed compressed monolayers, indicating substantial molecular deformation. As pH approached the isoelectric point (pH 8.0), a unique bilayer architecture emerged, with a densely packed inner layer supporting a more diffuse and non\u2010deformed outer layer. Notably, this pH\u2010induced structural reorganization was primarily driven by the Fc region, while the Fab fragments maintained consistent monolayer conformations regardless of pH conditions. Our work has established a quantitative framework for illustrating antibody\u2010surface interactions and the contribution of individual fragments in the adsorption process. This mechanistic understanding opens new avenues for enhancing the stability of antibody\u2010based pharmaceuticals on silicone oil\u2010coated delivery devices.<\/jats:p>","DOI":"10.1002\/smtd.202501717","type":"journal-article","created":{"date-parts":[[2026,2,12]],"date-time":"2026-02-12T09:29:57Z","timestamp":1770888597000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Domains Dictate Antibody Adsorption Architectures at Biocompatible Interfaces: Elucidation by QCM\u2010D and Neutron Reflectometry"],"prefix":"10.1002","volume":"10","author":[{"ORCID":"https:\/\/orcid.org\/0000-0003-0817-9140","authenticated-orcid":false,"given":"Kangcheng","family":"Shen","sequence":"first","affiliation":[{"name":"Biological Physics Laboratory Department of Physics and Astronomy The University of Manchester Manchester 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