KMP2

KMP2 (KISS1 Manufactured Peptide 2) is a peptide fragment of the KISS1 metastasis suppressor protein, specifically encompassing the N-terminal amino acid sequence from methionine-1 to arginine-56 (M1-R56). Developed by researchers at the University of Kansas Medical Center, KMP2 was identified during investigations into the extracellular processing of KISS1 and its role in suppressing cancer metastasis. While the canonical kisspeptin, Kisspeptin-54 (KP54), mediates its effects through the G-protein coupled receptor KISS1R (GPR54), KMP2 lacks the KISS1R binding motif. Despite this, KMP2 has demonstrated the ability to completely suppress metastatic colonization in vivo in murine melanoma models. Its mechanism of action involves inhibiting cell motility and modulating metabolic phenotypes, such as increasing mitochondrial biomass and elevating oxidative phosphorylation. These findings suggest that KMP2 operates through a novel, KISS1R-independent pathway, making it a potential therapeutic candidate for preventing metastatic spread in solid tumors.

Other names

KISS1 Manufactured Peptide 2KISS-1 Manufactured Peptide 2KISS 1 Manufactured Peptide 2KISS1 (1-56)