The adsorption of lysine vasopressin at ionized interfaces.
It has been shown by surface potential measurements that lysine vasopressin and oxytocin may be bound by ionic surfaces to very varied extents. To dodecyl sulphate and phosphatidylserine monolayers the binding is very strong and is comparable to that for biological receptors such as those in toad bladder. For dioleyl phosphate and the carboxyl group of the polypeptide alamethicin, the binding is rather weaker while, for the zwitterionic lipids phosphatidylcholine and phosphatidylethanolamine, and for the erythrocyte surface, which contains two varieties of carboxylic acid group, no interaction seems to take place. In no system does the lysyl amino group of the vasopressin appear necessary for adsorption and, in the dodecyl sulphate monolayers, the interaction is strong even when the ionization of the terminal alpha-amino group is suppressed.
D000818:Animals; D001001:Anura; D001665:Binding Sites; D007700:Kinetics; D008236:Lypressin; D008433:Mathematics; D008564:Membrane Potentials; D008567:Membranes, Artificial; D008954:Models, Biological; D010121:Oxytocin; D010718:Phosphatidylserines; D011199:Potentiometry; D012967:Sodium Dodecyl Sulfate; D013816:Thermodynamics; D001743:Urinary Bladder / Q000502:physiology; D014667:Vasopressins / Q000031:analogs & derivatives
D008567:Membranes, Artificial; D010718:Phosphatidylserines; D014667:Vasopressins; D012967:Sodium Dodecyl Sulfate; D010121:Oxytocin; D008236:Lypressin