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   <subfield code="a">(NATIONALLICENCE)springer-10.1007/PL00000695</subfield>
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   <subfield code="a">Unordered structure of proinsulin C-peptide in aqueous solution and in the presence of lipid vesicles</subfield>
   <subfield code="h">[Elektronische Daten]</subfield>
   <subfield code="c">[M. Henriksson*, J. Shafqat, E. Liepinsh, M. Tally, J. Wahren, H. Jörnvall, J. Johansson]</subfield>
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   <subfield code="a">Abstract.: Proinsulin C-peptide ameliorates renal and autonomic nerve function and increases skeletal muscle blood flow, oxygen uptake and glucose transport in patients with insulin-dependent diabetes mellitus. These effects have in part been ascribed to the stimulatory influence of C-peptide on Na+,K+-ATPase and endothelial nitric oxide synthase. To evaluate the capacity of C-peptide to insert into lipid bilayers and form ion channels, C-peptide secondary structure and membrane interactions were studied with circular dichroism spectroscopy and size exclusion chromatography. C-peptide is shown to lack a stable secondary structure, both when part of proinsulin and when free in aqueous solution, although the N-terminal third of the peptide exhibits an α-helical conformation in trifluoroethanol. Moreover, C-peptide remains disordered in the aqueous solvent in the presence of lipid vesicles, regardless of vesicle composition. In conclusion, C-peptide is unlikely to elicit physiological effects through stable conformation-dependent interactions with lipid membranes.</subfield>
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   <subfield code="a">Birkhäuser Verlag Basel,, 2000</subfield>
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   <subfield code="a">Key words. Diabetes mellitus</subfield>
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   <subfield code="a">protein secondary structure</subfield>
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   <subfield code="a">circular dichroism</subfield>
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   <subfield code="u">Department of Medical Biochemistry and Biophysics, Karolinska Institutet, S-17177 Stockholm (Sweden), Fax +46 8 337462, e-mail: mikael.henriksson@mbb.ki.se, SE</subfield>
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