Peptide models for protein-mediated cation transport.
Substances which can perturb the transmembrane cation balance in a predictable manner have wide-ranging uses in the study of cellular processes. We have undertaken to examine transmembrane calcium transport on the molecular level through the design and synthesis of a series of ionophoric peptides as models for protein-mediated calcium transport. General mechanisms for carrier-mediated membrane transport are discussed. Cation transport profiles are presented for transport by synthetic peptides of structure cyclo(Glu(OR)-Sar-Gly-(N-R1)-Gly)2, where R = benzyl ester or H; R1 = n-decyl or cyclohexyl. Transport of physiologically abundant cations across "liquid membranes" in Pressman cells mediated by cyclo(Glu-Sar-Gly-(N-decyl)Gly)2 was observed to be essentially calcium specific, as long as calcium ions were present in the system. Multilamellar and unilamellar phosphatidylcholine vesicles were each found to be emptied of internal 45Ca2+ ions upon addition of cyclo(Glu(OBz)-Sar-Gly-(N-cyclohexyl)Gly)2 to the vesicle suspension. The results are compared with the naturally occurring calcium ionophore A23187.
D001693:Biological Transport, Active; D000001:Calcimycin; D002118:Calcium / Q000378:metabolism; D002412:Cations; D008081:Liposomes; D008567:Membranes, Artificial; D008954:Models, Biological; D009842:Oligopeptides; D010713:Phosphatidylcholines
D002412:Cations; D008081:Liposomes; D008567:Membranes, Artificial; D009842:Oligopeptides; D010713:Phosphatidylcholines; D000001:Calcimycin; D002118:Calcium