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Matrix metalloproteinases (MMPs) belong to a family of proteases that play a crucial role in tissue remodeling and repair by degrading extracellular matrix proteins to enable cell migration. MMP-3 (also known as stromelysin-1) is thought to play a role in the vascular remodeling that occurs during aneurysm formation and may also be involved in wound repair, progression of atherosclerosis, and tumor initiation. MMP-3 inhibitor VIII is a cell permeable sulfonamide-based hydroxamic acid that binds to the active site of MMP-3 (K_i = 23 nM) and prevents its activity. This compound has also been shown to inhibit mouse macrophage metalloelastase MME/MMP-12 with an IC₅₀ value of 13 nM.

MMP12-IN-3 (compound 32) is a potent MMP12 inhibitor with an IC50 value of 4.9 nM. MMP12-IN-3 has the potential for the research of chronic respiratory diseases such as emphysema[1].

MMP-12: 4.9 nM (IC₅₀)

[1] Jeng AY, et al. Sulfonamide-based hydroxamic acids as potent inhibitors of mouse macrophage metalloelastase. Bioorg Med Chem Lett. 1998 Apr 21;8(8):897-902. DOI:10.1016/s0960-894x(98)00142-5