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Updated: Jul 15, 2026

Electrophoretic Crystallization of Ultrathin High-performance Metal-organic Framework Membranes
Published on: August 16, 2018
Protein refolding assisted by periodic mesoporous organosilicas
Xiqing Wang1, Diannan Lu, Rebecca Austin
1Department of Chemistry, University of California, Riverside, California 92521, USA.
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).
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