Synthesis of Cardiolipin Analogs and Characterization of Their Effects on Induction of the Peroxidase Activity of Cytochrome c

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Cardiolipin(CL) is a major phospholipid found in mammalian mitochondria with a multitude of biological functions. Activation of the peroxidase activity of cytochrome c(cyt c) by CL and hydrogen peroxide in mitochondria has been suggested to be a key event in early apoptosis stage. We have developed the concise procedure for the synthesis of CL. With numerous CLs in hand, we examined the structural factors of CL required for the formation and the induction of peroxidase activity of cyt c-CL complex in liposomal system. The activation efficiencies of CLs are well correlated with the binding affinities to cyt c. Our results revealed that at low CL content, the saturated acyl chain of CL is favorable for the activation of peroxidase activity of CL-bound cyt c and the proposed critical role of double bond in the acyl chains is not a general feature of the cyt c-CL interaction.