Ionophore A23187 disrupts membrane structure by modifying protein-lipid interactions.
The physiological function of membrane-boudn protein clearly depends on the nature of its neighbouring lipid. However, the question of how critical the protein is to the structure and function of membrane lipid has received much less attention. There is some evidence that lipid surrounding membrane protein, 'boundary lipid', may be more ordered than continuum lipid. Protein can also alter the enthalpy and temperature of pure lipid-phase transitions. However, controversy surrounds the question of whether membrane proteins determine long-range aspects of lipid structure or merly perturb their local environments. Here, we demonstrate that a lipophilic substance, the calcium ionophore, A23187 (Lilly), dramatically disorders the lipid structure of the membrane and that this phenomenon depends on the presence of proteins.
D000818:Animals; D000900:Anti-Bacterial Agents / Q000494:pharmacology*; D000001:Calcimycin / Q000494:pharmacology*; D002462:Cell Membrane / Q000187:drug effects*; D005454:Fluorescence Polarization; D008214:Lymphocytes / Q000187:drug effects / Q000648:ultrastructure; D008560:Membrane Fluidity / Q000187:drug effects; D008563:Membrane Lipids; D008565:Membrane Proteins; D051379:Mice
D000900:Anti-Bacterial Agents; D008563:Membrane Lipids; D008565:Membrane Proteins; D000001:Calcimycin