Cytotoxic effect of the immunotoxin constructed of the ribosome-inactivating protein curcin and the monoclonal antibody against Her2 receptor on tumor cells

Lidia Patricia Jaramillo-Quintero, Arturo Contis Montes De Oca, Andrés Romero Rojas, Saúl Rojas-Hernández, Rafael Campos-Rodríguez, Alma Leticia Martínez-Ayala

Research output: Contribution to journalArticlepeer-review

11 Scopus citations

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.

Original languageEnglish
Pages (from-to)896-906
Number of pages11
JournalBioscience, Biotechnology and Biochemistry
Volume79
Issue number6
DOIs
StatePublished - 2015

Keywords

  • Breast cancer
  • Chemical conjugation
  • ErBB2
  • Reductive amination
  • Targeted therapy

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