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TitleSolution structures of long-acting insulin analogues and their complexes with albumin.
Journal, issue, pagesActa Crystallogr D Struct Biol, Vol. 75, Issue Pt 3, Page 272-282, Year 2019
Publish dateMar 1, 2019
AuthorsLine A Ryberg / Pernille Sønderby / Fabian Barrientos / Jens T Bukrinski / Günther H J Peters / Pernille Harris /
PubMed AbstractThe lipidation of peptide drugs is one strategy to obtain extended half-lives, enabling once-daily or even less frequent injections for patients. The half-life extension results from a combination of ...The lipidation of peptide drugs is one strategy to obtain extended half-lives, enabling once-daily or even less frequent injections for patients. The half-life extension results from a combination of self-association and association with human serum albumin (albumin). The self-association and association with albumin of two insulin analogues, insulin detemir and insulin degludec, were investigated by small-angle X-ray scattering (SAXS) and dynamic light scattering (DLS) in phenolic buffers. Detemir shows concentration-dependent self-association, with an equilibrium between hexamer, dihexamer, trihexamer and larger species, while degludec appears as a dihexamer independent of concentration. The solution structure of the detemir trihexamer has a bent shape. The stoichiometry of the association with albumin was studied using DLS. For albumin-detemir the molar stoichiometry was determined to be 1:6 (albumin:detemir ratio) and for albumin-degludec it was between 1:6 and 1:12 (albumin:degludec ratio). Batch SAXS measurements of a 1:6 albumin:detemir concentration series revealed a concentration dependence of complex formation. The data allowed the modelling of a complex between albumin and a detemir hexamer and a complex consisting of two albumins binding to opposite ends of a detemir dihexamer. Measurements of size-exclusion chromatography coupled to SAXS revealed a complex between a degludec dihexamer and albumin. Based on the results, equilibria for the albumin-detemir and albumin-degludec mixtures are proposed.
External linksActa Crystallogr D Struct Biol / PubMed:30950398
MethodsSAS (X-ray synchrotron)
Structure data

SASDE26:
Albumin-insulin degludec 1:12 complex (Human Albumin (Recombumin(R) Elite, Albumedix Ltd.) + Insulin degludec(Tresiba(R), Novo Nordisk A/S))
Method: SAXS/SANS

SASDEV5:
Insulin detemir tri-hexamer (Insulin detemir)
Method: SAXS/SANS

SASDEW5:
Albumin-insulin detemir 1:6 complex, binding in Südlow's Site II
Method: SAXS/SANS

SASDEX5:
Albumin-insulin detemir 1:6 complex, binding in Südlow's Site I
Method: SAXS/SANS

SASDEY5:
Albumin-insulin detemir 2:12 complex, P1 symmetry (Human Albumin (Recombumin(R) Alpha, Albumedix Ltd.) + Insulin detemir (Levemir(R), Novo Nordisk A/S))
Method: SAXS/SANS

SASDEZ5:
Albumin-insulin detemir 2:12 complex, P2 symmetry (Human Albumin (Recombumin(R) Alpha, Albumedix Ltd.) + Insulin detemir (Levemir(R), Novo Nordisk A/S))
Method: SAXS/SANS

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