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TitleStructural basis of insulin fibrillation.
Journal, issue, pagesSci Adv, Vol. 9, Issue 37, Page eadi1057, Year 2023
Publish dateSep 15, 2023
AuthorsLiwei Wang / Catherine E Hall / Emiko Uchikawa / Dailu Chen / Eunhee Choi / Xuewu Zhang / Xiao-Chen Bai /
PubMed AbstractInsulin is a hormone responsible for maintaining normal glucose levels by activating insulin receptor (IR) and is the primary treatment for diabetes. However, insulin is prone to unfolding and ...Insulin is a hormone responsible for maintaining normal glucose levels by activating insulin receptor (IR) and is the primary treatment for diabetes. However, insulin is prone to unfolding and forming cross-β fibers. Fibrillation complicates insulin storage and therapeutic application. Molecular details of insulin fibrillation remain unclear, hindering efforts to prevent fibrillation process. Here, we characterized insulin fibrils using cryo-electron microscopy (cryo-EM), showing multiple forms that contain one or more of the protofilaments containing both the A and B chains of insulin linked by disulfide bonds. We solved the cryo-EM structure of one of the fibril forms composed of two protofilaments at 3.2-Å resolution, which reveals both the β sheet conformation of the protofilament and the packing interaction between them that underlie the fibrillation. On the basis of this structure, we designed several insulin mutants that display reduced fibrillation while maintaining native IR signaling activity. These designed insulin analogs may be developed into more effective therapeutics for type 1 diabetes.
External linksSci Adv / PubMed:37713485 / PubMed Central
MethodsEM (single particle)
Resolution3.2 Å
Structure data

40305

8sbd

EMDB-40305, PDB-8sbd:
Cryo-EM structure of insulin amyloid-like fibril that is composed of two antiparallel protofilaments
Method: EM (single particle) / Resolution: 3.2 Å

Source
  • homo sapiens (human)
KeywordsSIGNALING PROTEIN / amyloid-like fibril

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