Inhibition of lysosomal cysteine proteases by chrysotherapeutic compounds: a possible mechanism for the antiarthritic activity of Au(I).

摘要: Abstract Although Au(I) complexes have been used to treat rheumatoid arthritis for over 75 years, their mechanism of action is still poorly understood. A family enzymes responsible joint destruction in arthritis, the cathepsins, has discussed as a possible biological target Au(I). In this study, inhibition cathepsins by known drugs and related compounds was investigated. The tested inhibited cathepsin activity with IC50 values low 600 nM. More typical were 50–200 μM range. gold are not extremely potent inhibitors, it likely that biologically relevant given high concentrations serum joints patients undergoing chrysotherapy. While there multiple targets vivo, would provide protection against hallmark one antiarthritic activity.