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Comparative kinetic investigation for the binding patterns of monovalent and bivalent antibodies to transferrin receptors on murine brain microvascular endothelial cells
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Pharmacy, Department of Pharmacy. (ProDDe)
2023 (English)Independent thesis Advanced level (degree of Master (Two Years)), 30 credits / 45 HE creditsStudent thesis
Abstract [en]

Drug delivery to the central nervous system remains an impeding obstacle for the development of biopharmaceuticals. To study this, targeting strategies by genetic fusion to a molecular Trojan horse are used by utilizing receptor-mediated transcytosis, such as those governed by the transferrin receptor. Even though this approach has been effective, limiting factors related to how antibodies bind with transferrin receptor has not been readily defined. To study this, a single chain fragment constant (Fc) conjugated to a scFv8D3 (scFc-scFv8D3) and a chimeric mouse IgG 8D3 were designed and produced by Morrison et al (2023). Using living microvascular endothelial cells expressing transferrin receptors, antibody binding was analyzed using LigandTracer. The kinetic rate constants ka (association rate constant), kd (dissociation rate constant) were extracted for scFc-scFv8D3 and the chimeric mouse IgG 8D3 using a 1:1 model with distinct differences in binding stability (kd). The chimeric mouse IgG 8D3 exhibited a KD (equilibrium dissociation constant) of 0.1 nM, with ka (association rate constant) of 3.38×104 (M-1 s-1) and kd (dissociation rate constant) of 3.72×10-6 (s-1). The fitting of scFc-scFv8D3 yielded a KD of 2.96 nM, ka 1.69×104 (M-1 s-1), and a faster kd of 5.49×10-5 (s-1). To gain insight into the intracellular behaviour of scFc-scFv8D3 and the chimeric mouse IgG 8D3, a pH-sensitive dye, pHrodo GreenTM succinimidyl ester (ThermoFisher) was conjugated to the antibodies. With the LigandTracer in 37°C, it was observed that the chimeric mouse IgG 8D3 (bivalent) significantly accumulated in an acidic milieu, characteristic of the late endosome or lysosome. This result is consistent with the idea of Transferrin-receptor cross-linking inducing a degradation pathway. The scFc-scFv8D3 (monovalent) internalization suggests a re-direction of transcellular trafficking away from an acidic milieu. These findings imply that the affinity and mode of binding of antibodies play a crucial role in determining their intracellular fate and trafficking pathways.

Place, publisher, year, edition, pages
2023. , p. 35
Keywords [en]
Biopharmaceuticals
National Category
Pharmaceutical Sciences
Identifiers
URN: urn:nbn:se:uu:diva-504406OAI: oai:DiVA.org:uu-504406DiVA, id: diva2:1766681
External cooperation
Ridgeview Instruments AB
Subject / course
Pharmacy
Educational program
Master Programme in Drug Discovery and Development
Presentation
(English)
Supervisors
Examiners
Available from: 2023-06-19 Created: 2023-06-13 Last updated: 2023-06-19Bibliographically approved

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