MMP-10 Inhibitors

Matrix metalloproteinases (MMPs) are a family of zinc-dependent endopeptidases involved in the breakdown of extracellular matrix (ECM) components, playing a crucial role in various physiological and pathological processes, including tissue remodeling, inflammation, and tumor metastasis. MMP-10, specifically, is known to degrade various components of the ECM and has been implicated in processes like wound healing and cancer progression. Inhibitors of MMP-10 are therefore of significant interest in controlling these processes. MMP-10 inhibitors typically function by targeting the zinc ion in the enzyme's active site, essential for its proteolytic activity. This approach is common among MMP inhibitors due to the reliance of these enzymes on zinc for their catalytic function. The inhibitors listed vary in specificity and mechanism. Broad-spectrum inhibitors like Marimastat and Ilomastat chelate the zinc ion in MMPs, thereby inhibiting several members of the MMP family, including MMP-10. More selective inhibitors like Prinomastat and UK-356618 offer targeted inhibition of MMP-10. Antibiotics such as Doxycycline and Minocycline, while primarily used for their antimicrobial properties, also exhibit MMP-10 inhibitory activity, showcasing the diverse functionality of these compounds.