2026-07-18T13:59:05Zhttps://docta.ucm.es/rest/oai/request
oai:docta.ucm.es:20.500.14352/1155402025-03-18T15:59:29Zcom_20.500.14352_14col_20.500.14352_15
Docta Complutense author Cuesta Martínez, Ángel author Sánchez-Martín, David author Blanco-Toribio, Ana author Villate, Maider author Enciso-Álvarez, Kelly author Álvarez-Cienfuegos, Ana author Sainz-Pastor, Noelia author Sanz, Laura author Blanco, Francisco J. author Álvarez-Vallina, Luis 2025-01-22T11:16:09Z 2025-01-22T11:16:09Z 2012-03 Cuesta ÁM, Sánchez-Martín D, Blanco-Toribio A, Villate M, Enciso-Álvarez K, Álvarez-Cienfuegos A, et al. Improved stability of multivalent antibodies containing the human collagen XV trimerization domain. mAbs [Internet]. marzo de 2012 [citado 22 de enero de 2025];4(2):226-32. Disponible en: http://www.tandfonline.com/doi/abs/10.4161/mabs.4.2.19140 1942-08621942-0870 10.4161/mabs.4.2.19140 https://hdl.handle.net/20.500.14352/115540 https://doi.org/10.4161/mabs.4.2.19140 We recently described the in vitro and in vivo properties of an engineered homotrimeric antibody made by fusing the N-terminal trimerization region of collagen XVIII NC1 domain to the C-terminus of a scFv fragment [trimerbody (scFv-NC1) 3; 110 kDa]. Here, we demonstrated the utility of the N-terminal trimerization region of collagen XV NC1 domain in the engineering of trivalent antibodies. We constructed several scFv-based trimerbodies containing the human type XV trimerization domain and demonstrated that all the purified trimerbodies were trimeric in solution and exhibited excellent antigen binding capacity. Importantly, type XV trimerbodies demonstrated substantially greater thermal and serum stability and resistance to protease digestion than type XVIII trimerbodies. In summary, the small size, high expression level, solubility and stability of the trimerization domain of type XV collagen make it the ideal choice for engineering homotrimeric antibodies for cancer detection and therapy. eng Attribution-NonCommercial-NoDerivatives 4.0 International Improved stability of multivalent antibodies containing the human collagen XV trimerization domain journal article 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