Effect of eel calcitonin glycosylation on incorporation and channel formation in planar phospholipid membranes.
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-GlcNAc, Ct14-GlcNAc, Ct20-GlcNAc, Ct26-GlcNAc) 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-GlcNAc > Ct14-GlcNAc = Ct20-GlcNAc > 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-GlcNAc = 0.49, Ct14-GlcNAc = 0.41, Ct20-GlcNAc = 0.36, Ct26-GlcNAc = 0.47). These aspects would be useful in managing peptide properties for biotechnological and therapeutic applications considering the physiological nature of this peptide.
Meleleo
Daniela
D
Dipartimento Farmaco-Biologico, Università degli Studi di Bari, I-70126 Bari, Italy.
Micelli
Silvia
S
Toma
Kazunori
K
Haneda
Katsuji
K
Gallucci
Enrico
E
D000595:Amino Acid Sequence; D000818:Animals; D002116:Calcitonin / Q000737:chemistry* / Q000378:metabolism*; D002462:Cell Membrane / Q000737:chemistry / Q000378:metabolism*; D002463:Cell Membrane Permeability; D004524:Eels; D006031:Glycosylation; D007473:Ion Channels / Q000096:biosynthesis* / Q000378:metabolism*; D008051:Lipid Bilayers / Q000737:chemistry / Q000378:metabolism*; D008969:Molecular Sequence Data; D010743:Phospholipids / Q000378:metabolism*; D017433:Protein Structure, Secondary
D007473:Ion Channels; D008051:Lipid Bilayers; D010743:Phospholipids; D002116:Calcitonin