Chaperon-like activity of nanogels and function as protein nano carrier

In the presence of GroEL (0.2 μM) or nanogels(0.2 μM), refolding of acid denatured GFP(0.05 μM) was arrested. Folding was resumed by addition of ATP (1.0 mM) for GroEL or methyl-β-cyclodextrin(3.7 mM) for nanogels. About 70 % of GFP in GroEL and about 90% of GFP in nanogels recovered native structure. In the presence of GroEL or ALP nanogel, refolding of urea denatured β-D-galactosidase was started by the dilution. About 50 % of β-D-galactosidase recovered to native structure in both systems of GroEL and dodecyl group-bearing pullulan (ALP) nanogel recovered to native structure. Even by the addition of methyl-β-cyclodextrin for CHP nanogels, only 15 % of β-D-galactosidase activity recovered. Hydrophobic groups in the nanogels significantly affect chaperon-like activity.