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Molecular interactions of proinsulin C-peptide
Mälardalen University, School of Sustainable Development of Society and Technology. Mälardalen University, Department of Biology and Chemical Engineering.
2008 (English)Independent thesis Advanced level (degree of Master (One Year)), 20 credits / 30 HE creditsStudent thesis
Abstract [en]

The proinsulin C-peptide has long been thought as a byproduct from the insulin synthesis were it promotes the folding of the A and B-chain of insulin, but several studies in the past decade has shown that C-peptide is a bioactive peptide that can be beneficial in preventing diabetes complications. Patients with type I diabetes mellitus that has received C-peptide doses has shown for example improved renal function, increased blood flow in skeletal muscle and stimulated glucose transport. The aim of this study was to investigate the inter- and intramolecular binding properties of the proinsulin C-peptide, and in particular to study if the peptide forms oligomers and how the oligomerization is affected by additatives such as metal ions, insulin and sodium chloride. A method to identify C-peptide by SDS- and Native PAGE was developed. Using this technique, proinsulin C-peptide was found to form oligomers in μM concentrations. The oligomerization was dependent on the concentration, time and temperature. Metal ions such as Mg+, Zn2+ and Fe2+ affected the oligomerization. Insulin was shown to affect the oligomeric states of the C-peptide and to promote its disaggregation. Oligomerization of C-peptide was also detected with Surface Plasmon Resonance. Further studies are needed to find out how these finding can relate to the bioactivity of C-peptide.

Place, publisher, year, edition, pages
2008. , p. 30
Keywords [en]
proinsulin C-peptide, diabetes type II, oligomerization, SDS-page, Biacore
National Category
Chemical Engineering
Identifiers
URN: urn:nbn:se:mdh:diva-5658OAI: oai:DiVA.org:mdh-5658DiVA, id: diva2:209985
Presentation
(English)
Uppsok
fysik/kemi/matematik
Supervisors
Examiners
Available from: 2009-04-21 Created: 2009-03-29 Last updated: 2009-04-21Bibliographically approved

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CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association-8th-edition
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf