In nature system, protein called �molecularchaperone� assist the folding of denatured and nascent proteins by inhibitingirreversible aggregation. GroEL, known as the typical chaperone, interacts withnonnative protein far stronger than with native protein. Recently, nanogelsthat could facilitate the protein folding are of significant interest asartificial chapereone. However, contribution of protein recognition process onits function of artificial chaperone is unclear. In this study, lysozyme wasselected as a model target protein. Poly-N-isopropyl acrylamide basednanogel particles (NPs), which recognize protein via combination ofelectrostatic and hydrophobic interaction, were prepared by incorporatingacrylic acid (AAc) and N-tert-butylacrylamide (TBAm) with various feedratios. Binding process of lysozyme to NPs was analyzed by quartz crystalmicrobalance (QCM). Lysozyme denatured by 6 M guanidine hydrochloride was 100times diluted in NPs solution (100 mM phosphate buffer (pH 7.4)) and incubatedfor 30 minute at 25�C. The formation of aggregation was effectively inhibitedwith increasing of feed ratios of TBAm and AAc. In this presentation,correlation between protein-binding process of NPs and facilitation of proteinrefolding by NPs will be discussed.

Correlation between protein binding process of nanogel particles and facilitation of protein refolding

248th National Meeting (2014)

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.