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[A molecular dynamics study of the interaction between domain I-BAR of the IRSp53 protein and negatively charged

O V Levtsova, I D Davletov, O S Sokolova

    Biofizika
    |May 6, 2011
    PubMed

    The methods of computer simulation in full-atomic and large-grain approximations have been used to study specific interactions of the isolated domain I-BAR of the actin-binding protein IRSp53 and model membranes containing neutral phospholipids, as well as membranes containing high amounts of negatively charged PI(4,5)P2 phospholipids. It has been shown that the I-BAR domain does not interact with neutral lipids but induces the bending of the synthetic membrane rich in negatively charged phospholipids. A clusterization of charged lipids on the surface of the membrane at the sites of its interaction with the protein has been observed. This indicates that the interaction of the I-BAR protein with negatively charged lipids is of electrostatic and hydrophobic nature.

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