title: Protein refolding assisted by periodic mesoporous organosilicas.
abstract: 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).
authors.affiliation: Department of Chemistry, University of California, Riverside, California 92521, USA.
authors.forename: Xiqing
authors.initials: X
authors.lastname: Wang
authors.forename: Diannan
authors.initials: D
authors.lastname: Lu
authors.forename: Rebecca
authors.initials: R
authors.lastname: Austin
authors.forename: Arun
authors.initials: A
authors.lastname: Agarwal
authors.forename: Leonard J
authors.initials: LJ
authors.lastname: Mueller
authors.forename: Zheng
authors.initials: Z
authors.lastname: Liu
authors.forename: Jianzhong
authors.initials: J
authors.lastname: Wu
authors.forename: Pingyun
authors.initials: P
authors.lastname: Feng
mesh_terms: 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*
chemical_list: D012821:Silanes; D011092:Polyethylene Glycols; C040733:tetraethoxysilane; D012822:Silicon Dioxide; D009113:Muramidase