Franco-Mateos, E.; Souza-Egipsy, V.; García-Estévez, L.; Pérez-García, J.; Gion, M.; Garrigós, L.; Cortez, P.; Saavedra, C.; Gómez, P.; Ortiz, C.; Cruz, V.L.; Ramos, J.; Cortés, J.; Vega, J.F. Exploring the Combined Action of Adding Pertuzumab to Branded Trastuzumab versus Trastuzumab Biosimilars for Treating HER2+ Breast Cancer. Int. J. Mol. Sci.2024, 25, 3940.
Franco-Mateos, E.; Souza-Egipsy, V.; García-Estévez, L.; Pérez-García, J.; Gion, M.; Garrigós, L.; Cortez, P.; Saavedra, C.; Gómez, P.; Ortiz, C.; Cruz, V.L.; Ramos, J.; Cortés, J.; Vega, J.F. Exploring the Combined Action of Adding Pertuzumab to Branded Trastuzumab versus Trastuzumab Biosimilars for Treating HER2+ Breast Cancer. Int. J. Mol. Sci. 2024, 25, 3940.
Franco-Mateos, E.; Souza-Egipsy, V.; García-Estévez, L.; Pérez-García, J.; Gion, M.; Garrigós, L.; Cortez, P.; Saavedra, C.; Gómez, P.; Ortiz, C.; Cruz, V.L.; Ramos, J.; Cortés, J.; Vega, J.F. Exploring the Combined Action of Adding Pertuzumab to Branded Trastuzumab versus Trastuzumab Biosimilars for Treating HER2+ Breast Cancer. Int. J. Mol. Sci.2024, 25, 3940.
Franco-Mateos, E.; Souza-Egipsy, V.; García-Estévez, L.; Pérez-García, J.; Gion, M.; Garrigós, L.; Cortez, P.; Saavedra, C.; Gómez, P.; Ortiz, C.; Cruz, V.L.; Ramos, J.; Cortés, J.; Vega, J.F. Exploring the Combined Action of Adding Pertuzumab to Branded Trastuzumab versus Trastuzumab Biosimilars for Treating HER2+ Breast Cancer. Int. J. Mol. Sci. 2024, 25, 3940.
Abstract
The binding activity of various trastuzumab biosimilars versus the branded trastuzumab towards the glycosylated extracellular domain of the HER2 target in the presence of pertuzumab was in-vestigated. We employed size exclusion chromatography with tetra-detection methodology to simultaneously determine absolute molecular weight, concentration, molecular size, and intrinsic viscosity. All trastuzumab molecules in solution exhibit analogous behavior in their binary action towards HER2 regardless of the order of addition of trastuzumab/pertuzumab. This analogous behavior of all trastuzumab molecules, including biosimilars, highlights the robustness and con-sistency of their binding activity towards HER2. Furthermore, the addition of HER2 to a mixture of trastuzumab and pertuzumab leads to increased formation of high-order HER2 complexes, up to concentrations of one order of magnitude higher than in the case of sequential addition. The observed increase suggests a potential synergistic effect between these antibodies, which could enhance their therapeutic efficacy in HER2-positive cancers. These findings underscore the im-portance of understanding the complex interplay between therapeutic antibodies and their target antigens, providing valuable insights for the development of more effective treatment strategies.
Keywords
HER2+ breast cancer, monoclonal antibodies, trastuzumab biosimilars.
Subject
Medicine and Pharmacology, Oncology and Oncogenics
Copyright:
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
,
,
,
*
