Abstract
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 Ca 2+ to anionic phospholipid monolayers, which indicates that the annexin V-bound Ca 2+ 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.
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Schedule a callMore From: Biochimica et Biophysica Acta (BBA) - Biomembranes
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