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Morphological Change of Cell Membrane by Interaction with Domain‐Swapped Cytochrome c Oligomers
Author(s) -
Junedi Sendy,
Yasuhara Kazuma,
Nagao Satoshi,
Kikuchi Junichi,
Hirota Shun
Publication year - 2014
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201300728
Subject(s) - monomer , hela , phospholipid , chemistry , cytochrome c , vesicle , membrane , biophysics , cell membrane , biochemistry , cell , mitochondrion , biology , organic chemistry , polymer
Monomeric cyt c has been reported to bind to the mitochondrial membrane by electrostatic and hydrophobic interactions with anionic phospholipids. We have previously shown that domain‐swapped oligomeric cyt c retains the secondary structure of the monomer, and its surface possesses a larger area and more charges compared to the monomer. However, the effect of oligomerization of cyt c on cells has yet to be revealed. Herein, we investigated the interaction of oligomeric cyt c with anionic phospholipid‐containing vesicles and the outer membrane of HeLa cells. Oligomeric cyt c interacted more strongly than monomeric cyt c with anionic phospholipid‐containing vesicles and the outer membrane of HeLa cells. Oligomeric cyt c induced lateral phase separation of lipids in LUVs and GUVs, thereby leading to membrane disruption, whereas monomeric cyt c did not. Morphological changes in HeLa cells resulted from interaction with oligomeric cyt c , but little from interaction with the monomer. These results show that domain‐swapped oligomeric proteins might exhibit properties different to those of monomer in cell systems.