Li_2024_Proc.Natl.Acad.Sci.U.S.A_121_e2403049121

Reference

Title : Engineered polymer nanoparticles as artificial chaperones facilitating the selective refolding of denatured enzymes - Li_2024_Proc.Natl.Acad.Sci.U.S.A_121_e2403049121
Author(s) : Li Y , Yin D , Lee SY , Lv Y
Ref : Proc Natl Acad Sci U S A , 121 :e2403049121 , 2024
Abstract :

Molecular chaperones assist in protein refolding by selectively binding to proteins in their nonnative states. Despite progress in creating artificial chaperones, these designs often have a limited range of substrates they can work with. In this paper, we present molecularly imprinted flexible polymer nanoparticles (nanoMIPs) designed as customizable biomimetic chaperones. We used model proteins such as cytochrome c, laccase, and lipase to screen polymeric monomers and identify the most effective formulations, offering tunable charge and hydrophobic properties. Utilizing a dispersed phase imprinting approach, we employed magnetic beads modified with destabilized whole-protein as solid-phase templates. This process involves medium exchange facilitated by magnetic pulldowns, resulting in the synthesis of nanoMIPs featuring imprinted sites that effectively mimic chaperone cavities. These nanoMIPs were able to selectively refold denatured enzymes, achieving up to 86.7% recovery of their activity, significantly outperforming control samples. Mechanistic studies confirmed that nanoMIPs preferentially bind denatured rather than native enzymes, mimicking natural chaperone interactions. Multifaceted analyses support the functionality of nanoMIPs, which emulate the protective roles of chaperones by selectively engaging with denatured proteins to inhibit aggregation and facilitate refolding. This approach shows promise for widespread use in protein recovery within biocatalysis and biomedicine.

PubMedSearch : Li_2024_Proc.Natl.Acad.Sci.U.S.A_121_e2403049121
PubMedID: 38691587

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Citations formats

Li Y, Yin D, Lee SY, Lv Y (2024)
Engineered polymer nanoparticles as artificial chaperones facilitating the selective refolding of denatured enzymes
Proc Natl Acad Sci U S A 121 :e2403049121

Li Y, Yin D, Lee SY, Lv Y (2024)
Proc Natl Acad Sci U S A 121 :e2403049121