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[11] The antioxidant activity of GHK might be particularly potent when compared to other endogenous peptides like carnosine and reduced glutathione, especially when considering its potential ability to counteract hydroxyl radicals in cell cultures

In another embodiment of the invention, lysosomal storage diseases (LSDs) are treated with one of the following targeted drugs or compounds based on drugs and compounds that cause reduction of lysosomal stored materials like glucocerebroside, sphingomyelin, ceramide, G Ml -ganglioside, G M2 -ganglioside, globoside, galactosylceramide, dermatan sulfate, heparan sulfate, keratan sulfate, sulfatides, mucopolysaccharides, sialyloligosaccharides, glycoproteins, sialyloligosaccharides, glycolipids, globotriaosylceramide, O-linked glycopeptides, glycogen, free sialic acid, fucoglyco lipids, fucosyloligosaccharides, mannosyloligosaccharides, aspartylglucosamine, cholesteryl esters, triglycerides, and ceroid lipofuscin pigments in lysosomal storage diseases, like Gaucher disease (stored glucocerebroside) using targeted enzyme replacement therapy with beta-glucocerebrosidase (e.g., imiglucerase (Cerezyme marketed by Genzyme) or velalglucerase (in development by Shire), gene- activated beta-glucocerebrosidase, or with substrate inhibition of glucosylceramide synthase with imino sugars (e.g., miglustat (Zavesca marketed by Actelion) = N-butyl- deoxynojirimycin (NB-DNJ), N-butyl-galactosyl-deoxynojirimycin (NB-DGJ), N-(5- adamantane-1-yl-methoxypentyl)- deoxynojirimycin (AMP-DNJ), N-(5-adamantane-l- yl-methhoxy-pentyl)deoxynojirimycin (AMP-DNM), or with Glucosylceramide analogs (e.g., Genz 112638: d-threo-ethylendioxyphenyl-2-palmitoylamino-3- pyrrilidino-propanol), or with chaperone therapy (e.g., isofagomine tartrate, AT2101, (to be marketed as Plicera by Amicus Therapeutics, chemical name: (3R, 4R, 5R)- 3,4-Dihydroxy-5-hydroxymethyl-piperidine)

Six waffles

According to our structural analysis, zinc binding to sites of types 1, 4 and 5 ( Table 3 ) results in this fragment localizing at the intermolecular interface of the resulting dimer/trimer, impeding its access to the receptor (Fig