Proteaseinteracting

Protease-interacting describes molecules that bind to and modulate proteases, enzymes that cleave peptide bonds. These interactions regulate proteolysis in processes such as digestion, immune function, coagulation, and tissue remodeling. Interacting partners include substrates, inhibitors, activators, cofactors, and adaptor proteins that alter a protease’s activity, specificity, or localization. Substrates are cleaved to yield peptides or signaling fragments. Inhibitors can be reversible or irreversible; examples include serpins for serine proteases and tissue inhibitors of metalloproteinases (TIMPs) for metalloproteases. Activators promote maturation or catalytic efficiency, such as zymogen activation. Cofactors, like metal ions for metalloproteases, support enzymatic function. Adaptor proteins scaffold proteases with defined substrates in specific cellular compartments, refining proteolytic networks. Interactions may occur at the active site or at exosites and allosteric regions, enabling selective regulation.

Protease-interacting networks are essential for homeostasis and disease. They govern digestion, antigen processing, coagulation cascades, and extracellular matrix remodeling. Dysregulation can contribute to cancer, neurodegeneration, or inflammatory disorders. Therapeutic strategies often target protease activity or their interactions, using inhibitors or modulators to tune proteolysis.

Methods to study interactions include affinity purification, co-immunoprecipitation, cross-linking mass spectrometry, activity-based protein profiling, and substrate profiling. Structural approaches such as X-ray crystallography and cryo-electron microscopy reveal how interactors engage proteases at the structural level.