Artificial chaperones: from conventional designs to smart systems
Source abstract
Abstract
Abstract Chaperones are essential for the functions of many biomacromolecules as they facilitate folding, stabilize conformation, and prevent aggregation. Considering the high cost, low availability, and poor in vitro stability of natural chaperones, the development of artificial chaperones has been in high demand. Here, artificial chaperones that mimic the chaperoning functions on proteins and nucleic acids are reviewed. Aspects of compositions and structures of artificial chaperones, ranging from low-molecular-weight chemical chaperones to high-molecular-weight polymeric chaperones to complex nanostructures, are described. Furthermore, smart artificial chaperones that function in response to various external stimuli are described, pointing out their great potential to enable designs of more complex and functional systems for applications in biology, medicine, and industry.
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Research context
OpenAlex topics: Heat shock proteins research · RNA Interference and Gene Delivery · thermodynamics and calorimetric analyses
SciVX discovery tags are terminology-based. OpenAlex topics are source-provided classifications.
References (77)
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