Artificial chaperones: from conventional designs to smart systems
2026-03-25
Wancheng Zhang, Atsushi Maruyama
NPG Asia Materials, Published online: 25 March 2026; doi:10.1038/s41427-026-00640-z Molecular chaperones are proteins that assist in the proper folding of biomolecules, preventing misfolding and aggregation that can lead to diseases and economic losses in protein production. This study explores the development of artificial chaperones as cost-effective and customizable alternatives to natural chaperones. Researchers have designed chemical and polymeric chaperones that mimic natural mechanisms, using hydrophobic and electrostatic interactions to guide folding. For example, polymeric chaperones like PLL-g-Dex enhance DNA hybridization and protein folding by reducing repulsion and stabilizing structures. These findings are significant as they demonstrate the potential of artificial chaperones to improve protein stability and function in various applications. The study suggests that future research should focus on creating smarter chaperone systems that respond to environmental stimuli, enhancing their utility in biotechnology and medical treatments. This summary was initially drafted using artificial intelligence, then revised and fact-checked by the author.