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Dynamic folding modulation generates FGF21 variant against diabetes.

Lei Zhu1, Hongxin Zhao1, Juanjuan Liu1

  • 1High Magnetic Field Laboratory, CAS Key Laboratory of High Magnetic Field and Ion Beam Physical Biology, Hefei Institutes of Physical Science, Chinese Academy of Sciences, Hefei, China.

EMBO Reports
|December 9, 2020
PubMed
Summary
This summary is machine-generated.

Fibroblast growth factor 21 (FGF21) structure was determined using NMR. A designed FGF21 chimera (FGF21SS) improved protein stability and metabolic disorder treatment potential.

Keywords:
FGF21NMRanti-diabetesdisulfide bond mutationfolding dynamics

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Metabolic Research

Background:

  • Fibroblast growth factor 21 (FGF21) regulates glucose and lipid metabolism, showing promise for type 2 diabetes mellitus (T2DM) treatment.
  • Limited structural and dynamic information has hindered FGF21-based drug development.

Purpose of the Study:

  • To determine the structure and dynamics of FGF21.
  • To design a more stable and effective FGF21 variant for T2DM therapy.

Main Methods:

  • Nuclear magnetic resonance (NMR) spectroscopy was used to determine FGF21 structure.
  • A novel FGF21-FGF19 chimera, FGF21SS, was designed and engineered.
  • Functional characterization involved in vitro assays and in vivo studies in ob/ob mice.

Main Results:

  • FGF21 exhibits a non-canonical flexible β-trefoil conformation impacting protein stability.
  • The designed FGF21SS chimera demonstrated enhanced thermostability without hepatocyte proliferation.
  • FGF21SS improved insulin sensitivity, reduced inflammation, and lowered blood glucose and insulin levels in mice.

Conclusions:

  • Rational design based on protein dynamics offers a viable strategy for developing FGF21-based therapeutics.
  • The FGF21SS chimera represents a promising candidate for T2DM treatment.