Protein refolding assisted by periodic mesoporous organosilicas.
Herein we report a new strategy for protein refolding by taking advantage of the unique surface and pore characteristics of ethylene-bridged periodic mesoporous organosilica (PMO), which can effectively entrap unfolded proteins and assist refolding by controlled release into the refolding buffer. Hen egg white lysozyme was used as a model protein to demonstrate the new method of protein refolding. Through loading of denatured proteins inside uniform mesoporous channels tailored to accommodate individual protein, protein aggregation was minimized, and the folding rate was increased. Poly(ethyleneglycol) (PEG)-triggered continuous release of entrapped denatured lysozyme allowed high-yield refolding with high cumulative protein concentrations. The new method enhances the oxidative refolding of lysozyme (e.g., over 80% refolding yield at about 0.6 mg/mL).
Wang
Xiqing
X
Department of Chemistry, University of California, Riverside, California 92521, USA.
Lu
Diannan
D
Austin
Rebecca
R
Agarwal
Arun
A
Mueller
Leonard J
LJ
Liu
Zheng
Z
Wu
Jianzhong
J
Feng
Pingyun
P
D009113:Muramidase / Q000737:chemistry*; D010084:Oxidation-Reduction; D011092:Polyethylene Glycols / Q000737:chemistry*; D011489:Protein Denaturation; D017510:Protein Folding; D012821:Silanes / Q000737:chemistry*; D012822:Silicon Dioxide / Q000737:chemistry*
D012821:Silanes; D011092:Polyethylene Glycols; C040733:tetraethoxysilane; D012822:Silicon Dioxide; D009113:Muramidase