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Cytotoxic effect of the immunotoxin constructed of the ribosome-inactivating protein curcin and the monoclonal antibody against Her2 receptor on tumor cells
Authors:Lidia Patricia Jaramillo-Quintero  Arturo Contis Montes de Oca  Andrés Romero Rojas  Saúl Rojas-Hernández  Rafael Campos-Rodríguez
Institution:1. Centro de Investigación en Biotecnología Aplicada (CIBA-IPN), Instituto Politécnico Nacional, Tepetitla, Mexico;2. Escuela Superior de Medicina (ESM-IPN), Instituto Politécnico Nacional, Casco de Santo Tomás, Mexico;3. Facultad de Estudios Superiores Cuautitlán (FES-Cuautitlán UNAM), Universidad Nacional Autónoma de México, Cuautitlán Izcalli, Mexico
Abstract:The toxicity of the curcin on cancer cells allows to consider this protein as the toxic component of an immunotoxin directed to Her2, which is associated with cancer. Reductive amination was proposed to conjugate curcin and an anti-Her2; the binding was tested using Polyacrylamide gel electrophoresis, western blot, and immunocytochemistry. The in vitro cytotoxicity of curcin and the immunotoxin was assessed on breast cancer cell lines SK-BR-3 (Her2+) and MDA-MB-231 (Her2?). IC50 values for curcin were 15.5 ± 8.3 and 18.6 ± 2.4 μg/mL, respectively, statistically equivalent (p < 0.05). While to the immunotoxin was 2.2 ± 0.08 for SK-BR-3 and 147.6 ± 2.5 μg/mL for MDA-MB-231. These values showed that the immunotoxin was seven times more toxic to the SK-BR-3 than curcin and eight times less toxic to the MDA-MB-231. The immunotoxin composed of curcin and an antibody against Her2 and constructed by reductive amination could be a therapeutic candidate against Her2+ cancer.
Keywords:ErbB2  chemical conjugation  reductive amination  targeted therapy  breast cancer
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