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The interaction of cytochrome c (cyt c) with natural and synthetic membranes is known to be a complex phenomenon, involving both protein and lipid conformational changes. In this paper, we combined infrared and fluorescence spectroscopy to study the structural transformation occurring to the lipid network of cardiolipin-containing large unilamellar vesicles (LUVs). The data, collected at increasing protein/lipid ratio, demonstrate the existence of a multi-phase process, which is characterized by: (i) the interaction of cyt c with the lipid polar heads; (ii) the lipid anchorage of the protein on the membrane surface; and (iii) a long-distance order/disorder transition of the cardiolipin acyl chains. Such effects have been quantitatively interpreted introducing specific order parameters and discussed in the frame of the models on cyt c activity reported in literature.


Francesca Ripanti, Almerinda Di Venere, Mariangela Cestelli Guidi, Martina Romani, Alessandra Filabozzi, Marina Carbonaro, Maria Cristina Piro, Federica Sinibaldi, Alessandro Nucara, Giampiero Mei. The Puzzling Problem of Cardiolipin Membrane-Cytochrome c Interactions: A Combined Infrared and Fluorescence Study. International journal of molecular sciences. 2021 Jan 29;22(3)

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PMID: 33572777

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