Abstract:
:Our study highlights the tight relationship between protein binding to monolayers and the phase-state of the phospholipids. Interaction of mitochondrial creatine kinase with phospholipidic membranes was analysed using a two-phase monolayer system containing anionic phospholipids under chain mismatch conditions. Monolayers were made up of mixtures of DMPC/DPPG or DPPC/DMPG containing 40% negatively charged phospholipids which is approximately the negative charge content of the mitochondrial inner membrane. Langmuir isotherms of these monolayers showed that they underwent a phase transition from a liquid expanded state to a liquid-condensed phase at about 2 mN/m and 5 mN/m respectively. Interface morphology modifications caused by injection of mtCK under these monolayers at low or high surface pressure were monitored by Brewster angle microscopy. This work provides evidence that the presence at the air/water interface of discrete domains with increased charge density, may lead to difference in partition of soluble proteins such as mtCK, interacting with the lipid monolayer. Conversely these proteins may help to organize charged phospholipid domains in a membrane.
journal_name
Biochimiejournal_title
Biochimieauthors
Vernoux N,Maniti O,Marcillat O,Vial C,Granjon Tdoi
10.1016/j.biochi.2009.03.014subject
Has Abstractpub_date
2009-06-01 00:00:00pages
752-64issue
6eissn
0300-9084issn
1638-6183pii
S0300-9084(09)00075-3journal_volume
91pub_type
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