Biological macromolecules must fold into native structures to gain functional activities. In living cells, proteins called molecular chaperones mediate productive folding by preventing undesired interactions and aggregation and by facilitating refolding of misfolded macromolecules into their bioactive forms. Inspired by natural molecular chaperones, artificial chaperones that mimic some features of their biological counterparts have been designed. This review describes recent progress in the development of artificial chaperones and their promising applications in enhancing macromolecular assembly of proteins, polypeptides, and nucleic acids.
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