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Cytochrome c Complexes with Cardiolipin Monolayer Formed under Different Surface Pressure
Margarita A Marchenkova1,2, Yulia A Dyakova1,2, Elena Yu Tereschenko1,2
1Shubnikov Institute of Crystallography of Russian Academy of Sciences , 119333 Moscow, Russian Federation.
Cytochrome c (Cytc) interaction with cardiolipin (CL) in mitochondria is key to apoptosis. This study reveals Cytc undergoes a conformational change, forming stratified structures that may lead to membrane pores and apoptosis.
Area of Science:
- Mitochondrial biophysics
- Apoptosis signaling pathways
- Protein-lipid interactions
Background:
- The complex of cytochrome c (Cytc) and cardiolipin (CL) is critical for apoptosis.
- Existing models propose Cytc binds to the bilayer surface or forms hydrophobic nanoparticles.
Purpose of the Study:
- To investigate the interaction between Cytc and CL monolayers.
- To bridge the gap between existing structural models of the Cytc-CL complex.
Main Methods:
- Studied Cytc interaction with Langmuir monolayers of CL.
- Analyzed surface pressure changes and surface area-surface pressure isotherms.
- Investigated protein-lipid film behavior during compression-expansion cycles.
Main Results:
- Cytc binding to CL monolayers followed a pseudo-first-order rate.
- Conformational transition of Cytc was observed, creating "stratified" protein with hydrophobic and hydrophilic regions.
- Ethanol accelerated Cytc adsorption, and hysteresis loops indicated conformational changes.
Conclusions:
- Cytc undergoes a conformational transition upon interaction with CL monolayers.
- This stratification may lead to membrane folding, pore formation, or reactive "bubbles" within bilayers.
- The findings offer insights into Cytc-CL's role in apoptosis and lipid peroxidation.
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