The effect of 5-(n-alk(en)yl) resorcinols from rye on membrane structure.
The increased membrane permeability for K+, glycerol and erythritol, and membrane lysis induced by alkyl and alkenyl resorcinols, respectively, might be due to the interaction with membrane proteins and the formation of reversed micelles. The 5-(n-alk(en)yl) resorcinols show a very high stability at the air/water interface. The molecular area is 0.28 and 0.37 nm2 (at 30 mN/m) for alkyl and alkenyl resorcinols from rye, respectively. Differential scanning calorimetry experiments show a miscibility of alk(en)yl resorcinols with phosphatidylcholines. Only for alkenyl resorcinols is a small reduction found in the free energy of dipalmitoyl phosphatidylcholine. Electron microscopy studies show protein patching in erythrocyte membranes after the addition of resorcinols. The resorcinol-induced K+ release is not influenced by the presence of proteolytic enzymes, but strongly reduced by bovine serum albumin and glycophorin. 31P-NMR measurements show the occurrence of an isotropic and hexagonal signal in egg phosphatidylcholine in the presence of about 30 mol% alk(en)yl resorcinol.
D000818:Animals; D002463:Cell Membrane Permeability / Q000187:drug effects; D004910:Erythrocyte Membrane / Q000187:drug effects* / Q000648:ultrastructure; D004912:Erythrocytes / Q000187:drug effects*; D066298:In Vitro Techniques; D008081:Liposomes; D008823:Micelles; D008854:Microscopy, Electron; D010713:Phosphatidylcholines; D011188:Potassium / Q000378:metabolism; D011817:Rabbits; D012118:Resorcinols / Q000494:pharmacology*; D012434:Secale; D013816:Thermodynamics
D008081:Liposomes; D008823:Micelles; D010713:Phosphatidylcholines; D012118:Resorcinols; D011188:Potassium