Metalloprotease inhibitor

Metalloprotease inhibitors are cellular inhibitors of the matrix metalloprotease (or metalloproteinase) family of proteins (MMP). Several other proteins have similar inhibitory effects, however none as effective (netrins, procollagen C-terminal proteinase enhancer (PCPE), reversion-inducing cysteine-rich protein with Kazal motifs (RECK) and tissue factor pathway inhibitor (TFPI-2)). They might have other biological activities which have yet been fully characterised.^[1]

There are three classes of commonly used inhibitors for metalloproteinases.

• In vitro, EDTA, 1,10-phenanthroline and other chelating compounds lower the concentration of metal to the point where the metal is removed from the enzyme active site.

• Classical lock and key inhibitors such as phosphoramidon and bestatin bind tightly by approximating the transition state of the hydrolysis of the peptide, preventing it from acting on other substrates.

• Protein inhibitors such as α2-macroglobulin are known to work with metalloproteinases.

References

1. Baker, Andrew; Dylan R. Edwards; Gillian Murphy (October 2002). "Metalloproteinase inhibitors: biological actions and therapeutic opportunities". J Cell Sci 115: 3719–3727. doi:10.1242/jcs.00063. Retrieved 19 February 2013.

External links

• cambridgemedchemconsulting entry
• Sigma product entry