Date published: 2026-4-1

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MMP-26 Inhibitors

MMP-26 inhibitors belong to a class of compounds specifically designed to target and inhibit the activity of matrix metalloproteinase-26 (MMP-26). MMP-26, also known as matrilysin-2, is an enzyme that belongs to the family of matrix metalloproteinases, which are involved in the breakdown and remodeling of the extracellular matrix in various physiological and pathological processes. MMP-26 is known to play a role in tissue remodeling and cell migration, and its dysregulation has been associated with certain diseases and conditions. The inhibitors of MMP-26 are designed to interact with the enzyme and prevent its proteolytic activity, which is responsible for degrading various components of the extracellular matrix. By inhibiting MMP-26, these compounds aim to regulate the enzymatic breakdown of matrix proteins, thereby modulating cellular processes that involve tissue remodeling and migration. The design of MMP-26 inhibitors often involves the consideration of the enzyme's three-dimensional structure and the identification of key binding sites or active sites targeted by the inhibitors. MMP-26 inhibitors can come in various chemical structures, including small molecules or peptides, and are typically designed with high specificity to selectively interact with MMP-26, avoiding interference with other closely related matrix metalloproteinases. These inhibitors can be synthesized or identified through various methods, such as high-throughput screening, virtual screening, and rational drug design. Research on MMP-26 inhibitors is essential for providing valuable insights into the regulation of extracellular matrix remodeling and its impact on cellular behavior.
Product NameCAS #Catalog #QUANTITYPriceCitationsRATING

GM 6001

142880-36-2sc-203979
sc-203979A
1 mg
5 mg
$77.00
$270.00
55
(1)

GM 6001 is a selective inhibitor of matrix metalloproteinase-26 (MMP-26), exhibiting a unique mechanism of action through its interaction with the enzyme's active site. This compound stabilizes the enzyme in an inactive conformation, effectively reducing its proteolytic activity. The presence of specific functional groups facilitates strong electrostatic interactions and hydrophobic contacts, enhancing its selectivity for MMP-26 while minimizing off-target effects. Its kinetic profile reveals a competitive inhibition pattern, underscoring its potential for precise modulation of MMP-26 activity.