Self-Assembly Nanochaperone with Tunable Hydrophilic-Hydrophobic Surface for Controlled Protein Refolding.

Nanochaperones (nChaps) have significant potential to inhibit protein aggregation and assist in protein refolding. The interaction between nChaps and proteins plays an important role in nChaps performing chaperone-like functions, but the interaction mechanism is remaining elusive. In this work, a series of nChaps with tunable hydrophilic-hydrophobic surfaces were prepared, and the process of nChaps-assisted denatured protein refolding was systematically explored. We found that appropriate hydrophilic-hydrophobic balance on the nChap surface is critical for enhancing protein renaturation. This was because only the optimal interaction between nChap and protein could simultaneously guarantee the suitable capture and sufficient release of client proteins. The findings in this work will provide an effective reference for the design of nChaps and contribute to the development of the potential of nChaps in the future. This article is protected by copyright. All rights reserved.