Advances in Self‐Assembly Artificial Chaperone for Protein Folding Regulation

Proteins play a pivotal role in life functions, with their accurate structures being the cornerstone for carrying out physiological activities. They must fold into well-defined three-dimensional conformations to attain functional activity. However, protein folding is inherently an error-prone process, and environmental stimuli can also disrupt the natural conformation of proteins. Misfolding and aggregates not only lead to the loss of protein functions but also cause harm to cells and may even result in the onset of severe diseases. In cells, the efficient folding of proteins relies on the assistance of a special class of proteins known as molecular chaperones. They can facilitate the correct folding of nascent proteins, inhibit protein-unstable misfolding, maintain the protein native conformations, and prevent the formation of toxic protein aggregates. Inspired by natural chaperones, researchers have been dedicated to designing and fabricating artificial chaperones that mimic the structures and functions of natural chaperones, enabling them to exhibit excellent chaperone-like activities in regulating protein folding. Self-assembly materials have emerged as powerful candidates for developing artificial chaperones due to their modifiable structures and properties. In this review, the recent research status of self-assembly artificial chaperones based on different interactions with client proteins is discussed, and the application prospects of customized artificial chaperones for specific proteins in relevant diseases are further explored. This article is categorized under: Nanotechnology Approaches to Biology > Nanoscale Systems in Biology.