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Bogdan Bancia. Structure of C peptide in water. Ad Astra, 2018.

Abstract: C-peptide is released from its precursors, preproinsulin and proinsulin, in the course of insulin biosynthesis. Proinsulin is converted by a process of enzymatic cleavage to insulin and C-peptide in the beta cells. Two endopeptidases, prohormone convertases 2 and 3 (PC2 and PC3), cleave proinsulin at Lys64-Arg65 and Arg31-Arg32 sites, producing C-peptide and insulin.

C-peptide was long thought to have no physiological effect on its own but recent data demonstrated that it binds with high affinity to cell surfaces, probably to G protein-coupled receptors, with subsequent activation of Ca2+-dependent intracellular signalling pathways and stimulation of Na,K-ATPase activities. It was further shown that C-peptide is a biologically active peptide hormone with beneficial effects on kidney and nerve function in type 1 diabetes.

The 1H resonances of the C-peptide have been assigned in TFE (trifluoroethanol) solution but not in water. Within this project, the 1H, 13C and 15N NMR resonances of the C-peptide were assigned using a 36 mM sample in 90% H2O/10% D2O. NOEs were observed only between the neighbouring residues, showing that the C-peptide adopts a random coil conformation in solution. T1 (1H) relaxation rates also were in agreement with a random coil conformation. The observed chemical shifts were compared to the chemical shifts predicted for random coil peptides. The differences between the observed and the predicted 1H chemical shifts were small, supporting the notion of a random coil conformation of the C-peptide in solution.

Bogdan Bancia - master thesis 2004

Keywords: C peptide

Posted by Bogdan Bancia


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