RT Journal Article
T1 Improved stability of multivalent antibodies containing the human collagen XV trimerization domain
A1 Cuesta Martínez, Ángel
A1 Sánchez-Martín, David
A1 Blanco-Toribio, Ana
A1 Villate, Maider
A1 Enciso-Álvarez, Kelly
A1 Álvarez-Cienfuegos, Ana
A1 Sainz-Pastor, Noelia
A1 Sanz, Laura
A1 Blanco, Francisco J.
A1 Álvarez-Vallina, Luis
AB 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.
PB Taylor & Francis
SN 1942-0862
SN 1942-0870
YR 2012
FD 2012-03
LK https://hdl.handle.net/20.500.14352/115540
UL https://hdl.handle.net/20.500.14352/115540
LA eng
NO 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
NO Ministerio de Ciencia e Innovación (España)
NO Comunidad Autónoma de Madrid
NO FEDER
NO Instituto de Salud Carlos III
DS Docta Complutense
RD 16 abr 2025