Previous studies have shown that different calcitonins interact with planar lipid membranes to form ion channels. in this study, glycosylation of eel calcitonin (eCt) at different positions (Ct3-GIcNAc, Ct14-GIcNAc, Ct2O-GIcNAc, Ct26-GIcNAc) is shown to preserve molecular structure and slightly change the energy of incorporation and channel formation in planar lipid bilayers made up of palmitoyl-oleoyl-phosphatidylcholine:dioleoyl phosphatidyl-glycerol (85:15, w:w). The voltage needed to form channels decreased as the attached carbohydrate moved toward the C-terminal (eCt = Ct3-GIcNAc > Ct14-GIcNAc = Ct20GIcNAc: > Ct26-GlcNAc). Interestingly, all the Cts tested maintain the characteristic voltage-conductance dependence found for other Cts, the only channel properties modified concern ion selectivity, that shift toward anion selectivity (eCt = 0.97, Ct3-GIcNAc = 0.49, Ct14-GIcNAc = 0.41, Ct20-GIcNAc = 0.36, Ct26-GIcNAc = 0.47). These aspects would be useful in managing peptide properties for biotechnological and therapeutic applications considering the physiological nature of this peptide. (c) 2005 Elsevier Inc. All rights reserved.
Effect of eel calcitonin glycosylation on incorporation and channel formation in planar phospholipid membranes
MELELEO, DANIELA ADDOLORATA;
2006-01-01
Abstract
Previous studies have shown that different calcitonins interact with planar lipid membranes to form ion channels. in this study, glycosylation of eel calcitonin (eCt) at different positions (Ct3-GIcNAc, Ct14-GIcNAc, Ct2O-GIcNAc, Ct26-GIcNAc) is shown to preserve molecular structure and slightly change the energy of incorporation and channel formation in planar lipid bilayers made up of palmitoyl-oleoyl-phosphatidylcholine:dioleoyl phosphatidyl-glycerol (85:15, w:w). The voltage needed to form channels decreased as the attached carbohydrate moved toward the C-terminal (eCt = Ct3-GIcNAc > Ct14-GIcNAc = Ct20GIcNAc: > Ct26-GlcNAc). Interestingly, all the Cts tested maintain the characteristic voltage-conductance dependence found for other Cts, the only channel properties modified concern ion selectivity, that shift toward anion selectivity (eCt = 0.97, Ct3-GIcNAc = 0.49, Ct14-GIcNAc = 0.41, Ct20-GIcNAc = 0.36, Ct26-GIcNAc = 0.47). These aspects would be useful in managing peptide properties for biotechnological and therapeutic applications considering the physiological nature of this peptide. (c) 2005 Elsevier Inc. All rights reserved.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
