AI Article Synopsis

  • Glucagon, a hormone important for treating low blood sugar, is unstable in water and can change its structure into potentially harmful forms.
  • The study focused on analyzing the secondary structure of glucagon using techniques like circular dichroism spectroscopy and 2D Nuclear Overhauser effect spectroscopy at both release and expiry.
  • Results showed consistent structure components across both synthetic and recombinant glucagon, indicating no significant differences in their stability over time.

Article Abstract

Glucagon, a 29-amino acid polypeptide hormone, is an essential therapeutic agent used in the emergency treatment of hypoglycemia. However, glucagon is inherently unstable in aqueous solution. While glucagon equilibrates between unordered and the secondary α-helix state in solution, it can quickly transform into a different secondary β-sheet-rich amyloid-like fibril/oligomer structure under various conditions. Since changes in the secondary structure of glucagon can cause significant impacts, structure analysis is necessary and essential to assess the safety of the product. This study analyzed the secondary structure of glucagon products at the release and at the expiry using circular dichroism spectroscopy (CD) and 2D Nuclear Overhauser effect spectroscopy (2D NOESY). In order to also determine if structural differences exist between glucagon produced through different manufacturing processes, synthetic and recombinant glucagon products were used and compared. The CD results indicated that for all release and expired glucagon products, the structure compositions were 14 to 16% α-helix, 17 to 19% β-strand, 14 to 15% Turn, and 53 to 54% Unordered. This was consistent with the 2D NOESY analysis which showed that both products had an approximate α-helix composition of 14 to 17%. Overall, there were no significant differences in terms of the secondary structure between synthetic and recombinant glucagon products both at the release and at the expiry.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC9696263PMC
http://dx.doi.org/10.3390/molecules27227805DOI Listing

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