Theraputic peptides targeting protiens required for EGFR retrograde trafficking
| Name | Peptide mimetic | Mechanism of action | Reference |
|---|---|---|---|
| PMIP | MUC1 c-tail | EGFR-Muc1 binding | Bitler et al. [77] |
| GO-201 | MUC1 c-tail | Binds Muc1 c-tail | Raina et al. [78] |
| GO-202 | MUC1 c-tail | Binds Muc1 c-tail | Raina et al. [78] |
| GO-203 | MUC1 c-tail | EGFR-Muc1 binding | Kharbanda et al. [79] |
| GO-203-NP | MUC1 c-tail nano particle | Increased cellular uptake of GO-203 peptide | Hasegawa et al. [82] |
| EJ-1 | EGFR JXM domain | EGFR dimerization, nuclear localization, calmodulin binding, basolateral targeting, mitochondrial localization | Hart et al. [84] |
| SAH5 | Hydrocarbon stapled EGFR JXM domain | EGFR dimerization, nuclear localization, calmodulin binding, basolateral targeting, mitochondrial localization | Maisel et al. [85] |
| cSNX1.3 | SNX1 Bar domain | EGFR-SNX1 binding | Atwell et al. [86] |
Peptides derived from MUC1 cytoplasmic tail, EGFR juxtamembrane (JXM) domain, and SNX1 have demonstrated anti-tumor effects in models of breast, prostate, glioblastoma, and lung cancer. PMIP, EGFR JXM-1 (EJ-1), stapled aromatic hydrocarbon EJ1-5 (SAH5), and cSNX1.3 have all been shown to directly inhibit the retrograde trafficking of EGFR. The GO peptides have been shown to inhibit the nuclear accumulation of MUC1 and inhibit the retrograde trafficking of EGFR
