IL13Rα2 D1 enantiomer peptide

The IL13Rα2 D1 enantiomer peptide (also known as D-D1) is a synthetic peptide therapeutic composed entirely of D-amino acids (sequence: GSETWKTIITKN). It is derived from the D1 binding domain of the interleukin-13 receptor alpha 2 (IL13Rα2), a tumor-associated antigen frequently overexpressed in glioblastoma and metastatic colorectal cancer. By utilizing D-amino acids, the peptide achieves high resistance to proteolytic degradation and improved in vivo stability compared to its native L-amino acid counterpart. Mechanistically, the peptide acts as a competitive antagonist that blocks the interaction between IL-13 and IL13Rα2, thereby inhibiting downstream oncogenic signaling through the FAK, Src, AKT, and ERK1/2 pathways. Developed by researchers at the Spanish National Research Council (CSIC), the peptide has demonstrated the ability to suppress cancer cell migration, invasion, and proliferation, and has shown significant survival benefits in preclinical models of metastatic colorectal cancer.

Other names

D-D1 peptideD-D-1 peptideD-D 1 peptideIL13Rα2 D1 peptide (D-enantiomer)GSETWKTIITKN (D-amino acids)