MMP Substrate

MCA-Lys-Pro-Leu-Gly-Leu-DNP-Dpa-Ala-Arg-NH2

Matrix Metalloproteases (MMPs) belongs to the zinc metalloprotease family M10. They are zinc-dependent, calcium-containing hydrolases.

Matrix Metalloproteases (MMPs) are involved in extracellular matrix (ECM) degradation. MMPs regulate cellular and disease processes. They are implicated in processes such as cell proliferation, migration, differentiation, angiogenesis, anti-inflammatory response, vasoconstriction, apoptosis and host defense. Dysregulation of MMP is associated with arthritis, ulcers, encephalomyelitis and cancer.

The peptide MCA-Lys-Pro-Leu-Gly-Leu-DNP-Dpa-Ala-Arg-NH2, or FS-6, is a fluorogenic substrate for several matrix metalloproteinases (MMPs). FS-6 is a water-soluble, modified form of the well-established MMP substrate FS-1, where a lysine residue has been added to the N-terminus of FS-1. The resulting FS-6 has been reported to give a peptide with improved kinetic properties for several MMPs, including MMP-1, MMP-8, MMP-13, and MMP-14, compared to FS-1. This MMP substrate has also been described as a particularly useful substrate for the zinc metalloproteinase tumor necrosis factor-α converting enzyme (TACE or ADAM-17). FS-6 can be used to measure metalloproteinase activity in tissue culture conditions, for example, on the surface of viable cells in situ.