Membranotropic properties of the surface active reagent 2,4,6 trichloro 3 pentadecylphenol (TCP C15) have been studied. In preliminary investigations it was found that TCP C15 acts as an uncoupler of oxidative phosphorylation, selectively interacting with a fraction of non equilibrium membrane bound protons that forms during the work of proton pumps. In this work we obtained the following results: (1) addi tional validation of the conclusions drawn from the previous experiments was acquired on modified prepara tions of liver mitochondria, in which the fraction of non equilibrium membrane bound protons did not form;(2) it was shown that binding of TCP C15 to the liposome surface increases its negative ζ potential; this proves that TCP C15 binds to the surface of membranes in the negatively charged state; (3) on the BLM model it was found that under constant electric field (90 mV) TCP C15 not only induces the transmembrane transfer of charge, but also induces a specific hydrogen ion affinity to the surface of lipid bilayer; (4) strong evidence of the ionophore activity of TCP C15 was obtained on the same model; this allowed us to get a full scheme of uncoupling mechanism of TCP C15 on mitochondria and to explain the action of a catalyst (HEPES, 20 mM), which blocks this mechanism.Keywords: mitochondria, proton pump, non equillibrium membrane bound protons, interphase binding of proton
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