Exploring the Combined Action of Adding Pertuzumab to Branded Trastuzumab versus Trastuzumab Biosimilars for Treating HER2+ Breast Cancer

Author:

Franco-Mateos Emma1,Souza-Egipsy Virginia1,García-Estévez Laura2,Pérez-García José345,Gion María6,Garrigós Laia3,Cortez Patricia7,Saavedra Cristina6,Gómez Patricia3ORCID,Ortiz Carolina3,Cruz Víctor L.1ORCID,Ramos Javier1,Cortés Javier348,Vega Juan F.1ORCID

Affiliation:

1. BIOPHYM, Department of Macromolecular Physics, Instituto de Estructura de la Materia, IEM-CSIC, C/Serrano 113 bis, 28006 Madrid, Spain

2. Breast Cancer Department, MD Anderson Cancer Center, 28033 Madrid, Spain

3. International Breast Cancer Center (IBCC), Pangaea Oncology, Quiron Hospital, 08017 Barcelona, Spain

4. Medica Scientia Innovation Research (MedSIR), 08018 Barcelona, Spain

5. Medica Scientia Innovation Research (MedSIR), Ridgewood, NJ 07450, USA

6. Medical Oncology Department, Ramón y Cajal University Hospital, 28034 Madrid, Spain

7. IOB, Institute of Oncology, 28007 Madrid, Spain

8. Faculty of Biomedical and Health Sciences, Department of Medicine, Universidad Europea de Madrid, 28670 Madrid, Spain

Abstract

The binding activity of various trastuzumab biosimilars versus the branded trastuzumab towards the glycosylated extracellular domain of the human epidermal growth factor receptor 2 (HER2) target in the presence of pertuzumab was investigated. 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 consistency 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 importance of understanding the complex interplay between therapeutic antibodies and their target antigens, providing valuable insights for the development of more effective treatment strategies.

Funder

FERO

Contigo contra el cancer de la mujer

CSIC

Publisher

MDPI AG

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