Enhanced disulphide bond stability contributes to the once-weekly profile of insulin icodec

Nat Commun. 2024 Jul 20;15(1):6124. doi: 10.1038/s41467-024-50477-9.

Abstract

Insulin icodec is a once-weekly insulin analogue that has a long half-life of approximately 7 days, making it suitable for once weekly dosing. The Insulin icodec molecule was developed based on the hypothesis that lowering insulin receptor affinity and introducing a strong albumin-binding moiety would result in a long insulin half-life, provided that non-receptor-mediated clearance is diminished. Here, we report an insulin clearance mechanism, resulting in the splitting of insulin molecules into its A-chain and B-chain by a thiol-disulphide exchange reaction. Even though the substitutions in insulin icodec significantly stabilise insulin against such degradation, some free B-chain is observed in plasma samples from minipigs and people with type 2 diabetes. In summary, we identify thiol-disulphide exchange reactions to be an important insulin clearance mechanism and find that stabilising insulin icodec towards this reaction significantly contributes to its long pharmacokinetic/pharmacodynamic profile.

MeSH terms

  • Animals
  • Diabetes Mellitus, Type 2* / blood
  • Diabetes Mellitus, Type 2* / drug therapy
  • Diabetes Mellitus, Type 2* / metabolism
  • Disulfides* / chemistry
  • Half-Life
  • Humans
  • Hypoglycemic Agents / administration & dosage
  • Hypoglycemic Agents / chemistry
  • Hypoglycemic Agents / pharmacokinetics
  • Insulin* / administration & dosage
  • Insulin* / chemistry
  • Insulin* / metabolism
  • Insulin* / pharmacokinetics
  • Male
  • Receptor, Insulin / metabolism
  • Sulfhydryl Compounds / chemistry
  • Swine
  • Swine, Miniature

Substances

  • Disulfides
  • Hypoglycemic Agents
  • Insulin
  • Receptor, Insulin
  • Sulfhydryl Compounds