Recruiting Unfolding Chaperones to Solubilize Misfolded Recombinant Proteins

Rayees U.H. Mattoo*, Pierre Goloubinoff

*Corresponding author for this work

Research output: Chapter in Book/Report/Conference proceedingChapterpeer-review


This chapter discusses the various mechanisms by which chemical chaperones, foldases, and unfolding molecular chaperones can prevent inclusion body (IB) formation in bacteria and convert in vivo, stable misfolded recombinant polypeptides into soluble active proteins. Osmolytes have been shown to inhibit in vitro protein aggregation during refolding of unfolded/misfolded proteins and can be considered as chemical chaperones standing first in line of the cellular defenses against stress-induced protein aggregation. The native folding of some polypeptides may be limited by unfavorable distribution between cis-and trans-prolines and by the formation of the wrong disulfide bonds, requiring assistance of folding enzymes of peptidyl prolyl isomerases (PPIs) and protein disulfide isomerases (PDIs), respectively. Most molecular chaperones can be classified as: (1) the small Hsps (IbpA/B), (2) the HSP90s (HtpG), (3) the HSP70s (DnaK), (4) the HSP104s (ClpB), and (5) the chaperonins HSP60. Hsp90s are among the most abundant proteins in human cells.

Original languageEnglish
Title of host publicationProtein Aggregation in Bacteria
Subtitle of host publicationFunctional and Structural Properties of Inclusion Bodies in Bacterial Cells
Number of pages13
ISBN (Electronic)9781118845363
ISBN (Print)9781118448526
StatePublished - 14 Apr 2014
Externally publishedYes


FundersFunder number
Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung140512


    • Inclusion bodies (IBs)
    • Molecular chaperones
    • Peptidyl prolyl isomerases (PPIs)
    • Protein disulfide isomerases (PDIs)
    • Recombinant proteins
    • Small Hsps (sHsps)


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