Mitochondrial creatine kinase interaction with cardiolipin-containing biomimetic membranes is a two-step process involving adsorption and insertion

作者：Maniti Ofelia; Lecompte Marie France; Marcillat Olivier; Vial Christian; Granjon Thierry^*

来源：European Biophysics Journal, 2010, 39(12): 1649-1655.

DOI：10.1007/s00249-010-0600-4

• Differential capacity
• Mitochondrial creatine kinase
• Cardiolipin
• Langmuir monolayers
• Protein-membrane binding

Mitochondrial creatine kinase (mtCK) binding to the mitochondrial inner membrane largely determines its biological functions in cellular energy homeostasis, mitochondrial physiology, and dynamics. The membrane binding mechanism is, however, not completely understood. Recent data suggest that a hydrophobic component is involved in mtCK binding to cardiolipin at the outer face of the inner mitochondrial membrane, in addition to the well known electrostatically driven process. In this manuscript, using an electrochemical method derived from alternating current polarography for differential capacity measurements, we distinctly reveal that protein-cardiolipin interaction has a two-step mechanism. For short incubation time, protein adsorption to the phospholipid charged headgroup was the only process detected, whereas on a longer time scale evidence of protein insertion was observed.

• 出版日期2010-11