An ultra-stable single-chain insulin analog resists thermal inactivation and exhibits biological signaling duration equivalent to the native protein

Thermal degradation of insulin complicates its delivery and use. Previous efforts to engineer ultra-stable analogs were confounded by prolonged cellular signaling in vivo, of unclear safety and complicating mealtime therapy. We therefore sought an ultra-stable analog whose potency and duration of ac...

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Vydáno v:J Biol Chem
Hlavní autoři: Glidden, Michael D., Aldabbagh, Khadijah, Phillips, Nelson B., Carr, Kelley, Chen, Yen-Shan, Whittaker, Jonathan, Phillips, Manijeh, Wickramasinghe, Nalinda P., Rege, Nischay, Swain, Mamuni, Peng, Yi, Yang, Yanwu, Lawrence, Michael C., Yee, Vivien C., Ismail-Beigi, Faramarz, Weiss, Michael A.
Médium: Artigo
Jazyk:Inglês
Vydáno: American Society for Biochemistry and Molecular Biology 2018
Témata:
Protein Structure and Folding
On-line přístup:https://ncbi.nlm.nih.gov/pmc/articles/PMC5766902/
https://ncbi.nlm.nih.gov/pubmed/29114035
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.M117.808626
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