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Superoxide dismutase (SOD) , in its copper/zinc form, is a primary antioxidant enzyme that neutralizes superoxide radicals and depends on bound copper for catalysis

When volatile, destructive molecules known as reactive oxygen species (ROS) or "free radicals"such as hydroxyl radicals (HO) and peroxynitritethreaten to damage cellular DNA, lipids, or proteins, glutathione steps in

Functional peptide 1 contains four key domains: a fibrin-binding CREKA sequence for thrombus targeting, a thrombin-cleavable linker (LTPRGWRLGGC) for controlled peptide release, a transferrin receptor-binding HAIYPRH motif for BBB penetration, and a hydrophobic metal-binding domain for stabilization

Moreover, this process may also involve the activation of cyclic AMP (cAMP), which plays a crucial role in cellular signaling