Molecular chaperones play critical
roles in biological functions.
They are closely involved in the maintenance of cell homeostasis,
proper folding of proteins and nucleic acids, and inhibition of irreversible
aggregation in denatured proteins. In addition to protein production,
molecular chaperone function is widely recognized as important for
peptide and protein drug delivery systems. Therefore, much effort
has been made in recent decades to develop chaperone-mimetic molecules
that have similar structures and biological functions to natural chaperones.
These artificial molecular chaperone systems have been demonstrated
to facilitate proper protein and nucleic acid folding, in addition
to the formation of higher-order structures of synthetic molecules.
Furthermore, the functions of these artificial systems show promising
clinical applications in drug delivery and biomolecule detection.
This topical review focuses on recent advances in the design, construction,
characterization, and potential applications of different artificial
molecular systems with distinct functional roles, such as the folding
of water-soluble and membrane proteins, nucleic acids, and the self-assembly
of synthetic molecules. Strategies used in the construction of some
artificial molecule chaperone systems for proteins (such as pairs
of amphiphilic molecules or self-assembled nanogels) and their applications
as biomaterials are described. Specific examples from each design
strategy are also highlighted to demonstrate the mechanisms, challenges,
and limitations of the different artificial molecular systems. By
highlighting the many new developments that have expanded the applications
of the artificial chaperones beyond protein folding, this review aims
to stimulate further studies on their design and applications.