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Cysteine-based protein folding modulators for trapping intermediates and misfolded forms.

Hayato Nishino1, Mai Kitamura1, Shunsuke Okada1

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Researchers designed cysteine-based modulators to control protein folding pathways. These compounds can trap proteins in non-native conformations via disulfide bonds, offering new ways to study misfolded proteins and diseases.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Protein Chemistry

Background:

  • Protein folding is crucial for biological function, with on-pathway intermediates yielding native structures and off-pathway intermediates leading to disease-associated non-native forms.
  • Investigating folding intermediates and misfolded proteins is vital for understanding disease mechanisms.

Purpose of the Study:

  • To develop novel cysteine-based molecular modulators for controlling protein folding pathways.
  • To investigate the use of these modulators in trapping proteins in non-native conformations.

Main Methods:

  • Synthesis of cysteine-containing dipeptides conjugated with amino acids bearing mono- and diamino-groups.
  • Application of these dipeptides in oxidative protein folding experiments, monitoring disulfide-bond formation and protein conformations.

Main Results:

  • Cysteine and oxidized glutathione promoted native protein folding.
  • The developed dipeptides accelerated disulfide-bond formation but significantly increased the yield of non-native protein isomers.
  • This indicates a molecular design for inducing non-native conformations through intermolecular disulfide bonds.

Conclusions:

  • The study presents a molecular design for cysteine-based protein-folding modulators.
  • These modulators facilitate the formation of non-native protein conformations via intermolecular disulfide bonds.
  • The reversible nature of disulfide bonds suggests potential for reversible trapping and refolding strategies for transient and misfolded protein forms.