Membrane dynamic site complexant

We revealed that Alac-acetogenins, a new class of inhibitors of bovine mitochondrial Complex I, act differently from ordinary inhibitors and that the site of inhibition by Alac-acetogenins is downstream of that by ordinary inhibitors. The unique inhibitory action of hydrophobic Alac-acetogenins may be closely associated with the dynamic function of the membrane domain of Complex I. 

Biological membranes fluidity order parameters lipid-protein interactions translational diffusion site accessibility structural changes membrane potentials complexes and binding energy-linked and light-induced changes effects of additives location of proteins lateral organization and dynamics... 

Transmission of extracellular signals to the cell interior is based on receptor-induced recruitment and assembly of proteins into signaling complexes at the inner leaflet of the plasma membrane. Protein-protein and protein-lipid interactions play a crucial role in the process in which molecular proximity in specially formed membrane subdomains provides the special and temporal constraints that are required for proper signaling. The phospholipid bilayer is not merely a passive hydrophobic medium for this assembly process, but is also a site where the lipid and the protein components are enriched by a dynamic process (see Chapter 5). 

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