Abstract
Momordica antiviral protein 30 kDa (MAP30) is a type I ribosome-inactivating protein (RIP) with antibacterial, anti-HIV and antitumor activities but lacks the ability to target tumor cells. To increase its tumor-targeting ability, the arginine-glycine-aspartic (RGD) peptide and the epidermal growth factor receptor interference (EGFRi) peptide were fused with MAP30, which was named ELRL-MAP30. The use of targeted therapy for triple-negative breast cancer (TNBC) MDA-MB-231 cells, which lack the expression of estrogen receptor (ER), Progesterone receptor (PgR) and human epidermal growth factor receptor-2 (HER2), is limited. In this study, we focused on exploring the effect and mechanism of ELRL-MAP30 on TNBC MDA-MB-231 cells. First, we discovered that ELRL-MAP30 significantly inhibited the migration and invasion of MDA-MB-231 cells and induced MDA-MB-231 cell apoptosis. Moreover, ELRL-MAP30 treatment significantly reduced Bcl-2 protein expression and increased BAX protein expression. Furthermore, ELRL-MAP30 triggered apoptosis via the Fak/EGFR/Erk and Ilk/Akt signaling pathways. In addition, recombinant ELRL-MAP30 can also inhibit chicken embryonic angiogenesis, indicating its potential therapeutic effects on tumor angiogenesis. Collectively, these results indicate that ELRL-MAP30 has significant tumor-targeting properties in MDA-MB-231 cancer cells and reveals potential therapeutic effects on angiogenesis. These findings indicate the potential role of ELRL-MAP30 in the targeted treatment of the TNBC cell line MDA-MB-231.