Chaperonins: Nanocarriers with Biotechnological Applications

Chaperonins are molecular chaperones found in all kingdoms of life, and as such they assist in the folding of other proteins. Structurally, chaperonins are cylinders composed of two back-to-back rings, each of which is an oligomer of similar to 60-kDa proteins. Chaperonins are found in two main conformations, one in which the cavity is open and ready to recognise and trap unfolded client proteins, and a closed form in which folding takes place. The conspicuous properties of this structure (a cylinder containing a cavity that allows confinement) and the potential to control its closure and aperture have inspired a number of nanotechnological applications that will be described in this review.

Automated summary

Chaperonins are molecular chaperones present in all kingdoms of life, assisting in the folding of other proteins. Structurally, they are cylinders composed of two back-to-back rings, with open and closed conformations for trapping client proteins and facilitating folding. Their unique structure and controllable aperture have led to various nanotechnological applications.