The tripeptide binds copper with high affinity (log stability constant of 16.44) and delivers it to tissue sites where copper-dependent enzymes (lysyl oxidase, superoxide dismutase, cytochrome c oxidase) drive collagen crosslinking, antioxidant defense, and mitochondrial respiration [1][2]
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Accessed March 15, 2016
Binding affinity of the GSSSG/LASSS-pretreated HGF ( bars 7 and 11 ) to c-met was significantly higher than that of nitrated HGF ( bar 3 , peroxynitrite-treated at 1:2000) and reached approximately 80% of the full activity of the positive controls exposed to untreated HGF ( bars 2 and 2 )