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-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.
journal_name
Peptidesjournal_title
Peptidesauthors
Meleleo D,Micelli S,Toma K,Haneda K,Gallucci Edoi
10.1016/j.peptides.2005.09.011subject
Has Abstractpub_date
2006-04-01 00:00:00pages
805-11issue
4eissn
0196-9781issn
1873-5169pii
S0196-9781(05)00465-1journal_volume
27pub_type
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