Interactions of annexin V with phospholipid monolayers.

To understand the mechanism of annexin V-membrane interactions, we measured the interaction of human recombinant annexin V with phospholipid monolayers with differing head group and acyl group structures. Annexin V interacted with anionic phospholipid monolayers via non-specific electrostatic interactions, which was highly dependent on the surface pressure of monolayer with a sharp maximum. The unique surface pressure dependence of the annexin V-monolayer binding is strikingly similar to that observed for the binding of Ca2+ to anionic phospholipid monolayers, which indicates that the annexin V-bound Ca2+ binds two phospholipids at the membrane surface and that factors governing the Ca(2+)-phospholipid complex formation regulate the overall annexin V-Ca(2+)-membrane interactions.