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 ~60-kDa proteins. Chaperonins are found in two main conformations,...

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Bibliographic Details
Published in:Nanomaterials (Basel, Switzerland) Switzerland), 2021-02, Vol.11 (2), p.503
Main Authors: Pipaón, Sergio, Gragera, Marcos, Bueno-Carrasco, M Teresa, García-Bernalt Diego, Juan, Cantero, Miguel, Cuéllar, Jorge, Fernández-Fernández, María Rosario, Valpuesta, José María
Format: Article
Language:English
Subjects:
Binding sites
Biotechnology
Cadmium selenide
Chaperones
Chaperonins
Folding
molecular chaperones
nanocarriers
Nanoparticles
nanoreactors
Nanotechnology
Proteins
Quantum dots
Review
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Summary: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 ~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.
ISSN:2079-4991
2079-4991
DOI:10.3390/nano11020503