Stable Monomeric Insulin Formulations Enabled by Supramolecular PEGylation of Insulin Analogues.

ABSTRACT: Current "fast-acting" insulin analogues contain amino acid modifications meant to inhibit dimer formation and shift the equilibrium of association states toward the monomeric state. However, the insulin monomer is highly unstable and current formulation techniques require insulin to primarily exist as hexamers to prevent aggregation into inactive and immunogenic amyloids. Insulin formulation excipients have thus been traditionally selected to promote insulin association into the hexameric form to enhance formulation stability. This study exploits a novel excipient for the supramolecular PEGylation of insulin analogues, including aspart and lispro, to enhance the stability and maximize the prevalence of insulin monomers in formulation. Using multiple techniques, it is demonstrated that judi

SUBMITTER: Maikawa CL 

PROVIDER: S-EPMC7079736 | biostudies-literature | 2020 Jan

REPOSITORIES: biostudies-literature