Cytosolic Interactome Protects Against Protein Unfolding in a Single Molecule Experiment

Barbara Scalvini, Laurens W.H.J. Heling, Vahid Sheikhhassani, Vanda Sunderlikova, Sander J. Tans, Alireza Mashaghi

Research output: Contribution to journalArticlepeer-review

1 Citation (Scopus)


Single molecule techniques are particularly well suited for investigating the processes of protein folding and chaperone assistance. However, current assays provide only a limited perspective on the various ways in which the cellular environment can influence the folding pathway of a protein. In this study, a single molecule mechanical interrogation assay is developed and used to monitor protein unfolding and refolding within a cytosolic solution. This allows to test the cumulative topological effect of the cytoplasmic interactome on the folding process. The results reveal a stabilization against forced unfolding for partial folds, which are attributed to the protective effect of the cytoplasmic environment against unfolding and aggregation. This research opens the possibility of conducting single molecule molecular folding experiments in quasi‐biological environments.
Original languageEnglish
Article number2300105
Number of pages10
JournalAdvanced Biology
Issue number12
Publication statusPublished - Dec 2023


  • protein folding
  • cytosol
  • single-molecule assay
  • optical tweezers
  • chaperone


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