Abstract
The interactions between amine local anesthetic dibucaine and pig erythrocyte membranes have been studied by proton and phosphorus-31 nuclear magnetic resonance (1H-and <31>P-NMR) spectroscopy. It was found that dibucaine, bound to the membranes, increases the mobility of the hydrophobic acyl chains of the phospholipids, but that it decreases the mobility and/or changes the structure of the polar headgroups. The interactions with peripheral membrane proteins, i.e., spectrin and actin, were found to be weak. These observations indicate that the dibucaine locates across the polar and hydrophobic areas of the lipid phase of the membranes by both electrostatic and hydrophobic interactions. It is assumed that the changes in the mobility and/or the conformation of the phospholipids residing around the Na channel protein are essential in causing anesthesia.
