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- W2133271843 endingPage "806" @default.
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- W2133271843 abstract "Insulin, a small peptide hormone, is crucial in maintaining blood glucose homeostasis. The stability and activity of the protein is directed by an intricate system involving disulfide bonds to stabilize the active monomeric species and by their non-covalent oligomerization. All known insulin variants in vertebrates consist of two peptide chains and have six cysteine residues, which form three disulfide bonds, two of them link the two chains and a third is an intra-chain bond in the A-chain. This classical insulin fold appears to have been conserved over half a billion years of evolution. We addressed the question whether a human insulin variant with four disulfide bonds could exist and be fully functional. In this review, we give an overview of the road to engineering four-disulfide bonded insulin analogs. During our journey, we discovered several active four disulfide bonded insulin analogs with markedly improved stability and gained insights into the instability of analogs with seven cysteine residues, importance of dimerization for stability, insulin fibril formation process, and the conformation of insulin binding to its receptor. Our results also open the way for new strategies in the development of insulin biopharmaceuticals." @default.
- W2133271843 created "2016-06-24" @default.
- W2133271843 creator A5005754454 @default.
- W2133271843 creator A5053745370 @default.
- W2133271843 creator A5065781837 @default.
- W2133271843 creator A5085997583 @default.
- W2133271843 date "2015-09-18" @default.
- W2133271843 modified "2023-10-08" @default.
- W2133271843 title "The road to the first, fully active and more stable human insulin variant with an additional disulfide bond" @default.
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- W2133271843 doi "https://doi.org/10.1002/psc.2822" @default.
- W2133271843 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/26382042" @default.
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