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MMPs are inhibited by molecules known as tissue inhibitor of metalloproteinases (TIMPs), which comprise a family of four protease inhibitors: TIMP-1, TIMP-2, TIMP-3, and TIMP-4. There are also synthetic inhibitors which generally work by binding the catalytic zinc atom at the MMP active site tightly and preventing catalysis. The common groups used for synthetic inhibition include hydroxamates, carboxylates, thiols, and phosphinyls. Hydroxymates are particularly potent inhibitors of MMPs and other zinc-dependent enzymes, due to their bidentate chelation of the zinc atom [5].