| Literature DB >> 33572777 |
Francesca Ripanti1, Almerinda Di Venere2, Mariangela Cestelli Guidi3, Martina Romani3, Alessandra Filabozzi4, Marina Carbonaro5, Maria Cristina Piro2, Federica Sinibaldi2, Alessandro Nucara1, Giampiero Mei2.
Abstract
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.Entities:
Keywords: cardiolipin; cytochrome c; membrane disorder; protein-membrane binding
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Year: 2021 PMID： 33572777 PMCID： PMC7866282 DOI： 10.3390/ijms22031334
Source DB: PubMed Journal: Int J Mol Sci ISSN： 1422-0067 Impact factor: 5.923