{"id":32355,"date":"2025-10-14T11:07:57","date_gmt":"2025-10-14T15:07:57","guid":{"rendered":"https:\/\/www.med.unc.edu\/biochem\/?p=32355"},"modified":"2025-10-28T11:10:43","modified_gmt":"2025-10-28T15:10:43","slug":"leiderman-lab-new-publication-in-jth","status":"publish","type":"post","link":"https:\/\/www.med.unc.edu\/biochem\/news\/leiderman-lab-new-publication-in-jth\/","title":{"rendered":"Leiderman lab new publication in JTH"},"content":{"rendered":"<p>The Leiderman lab published &#8220;Mathematical analysis of emicizumab: affinity-driven complex formation and lipid-surface reactions&#8221; in the Journal of Thrombosis and Haemostasis.<\/p>\n<p><img loading=\"lazy\" decoding=\"async\" class=\"alignnone wp-image-32356 size-large\" src=\"https:\/\/www.med.unc.edu\/biochem\/wp-content\/uploads\/sites\/795\/2025\/10\/new-L-lab-photo-fall-2025-1024x652.jpg\" alt=\"The Leiderman lab photo\" width=\"1024\" height=\"652\" srcset=\"https:\/\/www.med.unc.edu\/biochem\/wp-content\/uploads\/sites\/795\/2025\/10\/new-L-lab-photo-fall-2025-1024x652.jpg 1024w, https:\/\/www.med.unc.edu\/biochem\/wp-content\/uploads\/sites\/795\/2025\/10\/new-L-lab-photo-fall-2025-300x191.jpg 300w, https:\/\/www.med.unc.edu\/biochem\/wp-content\/uploads\/sites\/795\/2025\/10\/new-L-lab-photo-fall-2025-768x489.jpg 768w, https:\/\/www.med.unc.edu\/biochem\/wp-content\/uploads\/sites\/795\/2025\/10\/new-L-lab-photo-fall-2025-600x382.jpg 600w, https:\/\/www.med.unc.edu\/biochem\/wp-content\/uploads\/sites\/795\/2025\/10\/new-L-lab-photo-fall-2025-560x357.jpg 560w, https:\/\/www.med.unc.edu\/biochem\/wp-content\/uploads\/sites\/795\/2025\/10\/new-L-lab-photo-fall-2025.jpg 1280w\" sizes=\"auto, (max-width: 1024px) 100vw, 1024px\" \/><\/p>\n<p>The bispecific antibody emicizumab is designed to replace the function of clotting factor VIII in hemophilia A by bridging factor IXa and factor X. In normal clotting, activated FVIII serves as a cofactor for FIXa, promoting FX activation by colocalizing the enzyme and substrate on lipid membranes. Our study shows that although emicizumab does not bind lipid, its activity is enhanced in the presence of lipid surfaces. Using experiments and mechanistic mathematical modeling, we demonstrate that emicizumab interacts with proteins already bound to the membrane, providing quantitative insight into its mechanism and informing the design of next-generation bispecific antibodies. Read more: https:\/\/www.sciencedirect.com\/science\/article\/pii\/S1538783625004258<\/p>\n","protected":false},"excerpt":{"rendered":"<p>The Leiderman lab published &#8220;Mathematical analysis of emicizumab: affinity-driven complex formation and lipid-surface reactions&#8221; in the Journal of Thrombosis and Haemostasis.<\/p>\n","protected":false},"author":41619,"featured_media":32356,"comment_status":"closed","ping_status":"closed","sticky":false,"template":"","format":"standard","meta":{"_acf_changed":false,"layout":"","cellInformation":"","apiCallInformation":"","footnotes":"","_links_to":"","_links_to_target":""},"categories":[2],"tags":[10],"class_list":["post-32355","post","type-post","status-publish","format-standard","has-post-thumbnail","hentry","category-news","tag-news_faculty","odd"],"acf":[],"yoast_head":"<!-- This site is optimized with the Yoast SEO plugin v26.8 - https:\/\/yoast.com\/product\/yoast-seo-wordpress\/ -->\n<title>Leiderman lab new publication in JTH | Biochemistry and Biophysics<\/title>\n<meta name=\"robots\" content=\"index, follow, max-snippet:-1, max-image-preview:large, max-video-preview:-1\" \/>\n<link rel=\"canonical\" href=\"https:\/\/www.med.unc.edu\/biochem\/news\/leiderman-lab-new-publication-in-jth\/\" \/>\n<meta property=\"og:locale\" content=\"en_US\" \/>\n<meta property=\"og:type\" content=\"article\" \/>\n<meta property=\"og:title\" content=\"Leiderman lab new publication in JTH | Biochemistry and Biophysics\" \/>\n<meta property=\"og:description\" content=\"The Leiderman lab published &quot;Mathematical analysis of emicizumab: affinity-driven complex formation and lipid-surface reactions&quot; 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