Please use this identifier to cite or link to this item:
https://doi.org/10.1038/s41467-017-01585-2
Title: | Thermostable exoshells fold and stabilize recombinant proteins | Authors: | Deshpande S. Masurkar N.D. Girish V.M. Desai M. Chakraborty G. Chan J.M. Drum C.L. |
Keywords: | green fluorescent protein horseradish peroxidase nanoparticle recombinant protein Renilla luciferin 2 monooxygenase thermostable protein nanoparticle unclassified drug recombinant protein gene expression nanoparticle protein shell stabilization Article controlled study drug release drug stability enzyme substrate fluorescence in vitro study nanoencapsulation nanoengineering nanotechnology nonhuman pH protein degradation protein denaturation protein expression protein folding protein metabolism protein tertiary structure stereospecificity thermostability titrimetry Archaeoglobus fulgidus biosynthesis chemistry Escherichia coli gene expression genetics metabolism physiology protein folding Armoracia rusticana Renilla luciferase Archaeoglobus fulgidus Escherichia coli Gene Expression Green Fluorescent Proteins Horseradish Peroxidase Luciferases, Renilla Nanoparticles Protein Folding Recombinant Proteins |
Issue Date: | 2017 | Publisher: | Nature Publishing Group | Citation: | Deshpande S., Masurkar N.D., Girish V.M., Desai M., Chakraborty G., Chan J.M., Drum C.L. (2017). Thermostable exoshells fold and stabilize recombinant proteins. Nature Communications 8 (1) : 1442. ScholarBank@NUS Repository. https://doi.org/10.1038/s41467-017-01585-2 | Abstract: | The expression and stabilization of recombinant proteins is fundamental to basic and applied biology. Here we have engineered a thermostable protein nanoparticle (tES) to improve both expression and stabilization of recombinant proteins using this technology. tES provides steric accommodation and charge complementation to green fluorescent protein (GFPuv), horseradish peroxidase (HRPc), and Renilla luciferase (rLuc), improving the yields of functional in vitro folding by ~100-fold. Encapsulated enzymes retain the ability to metabolize small-molecule substrates, presumably via four 4.5-nm pores present in the tES shell. GFPuv exhibits no spectral shifts in fluorescence compared to a nonencapsulated control. Thermolabile proteins internalized by tES are resistant to thermal, organic, chaotropic, and proteolytic denaturation and can be released from the tES assembly with mild pH titration followed by proteolysis. © 2017 The Author(s). | Source Title: | Nature Communications | URI: | https://scholarbank.nus.edu.sg/handle/10635/174485 | ISSN: | 2041-1723 | DOI: | 10.1038/s41467-017-01585-2 |
Appears in Collections: | Elements Staff Publications |
Show full item record
Files in This Item:
File | Description | Size | Format | Access Settings | Version | |
---|---|---|---|---|---|---|
10_1038_s41467-017-01585-2.pdf | 1.96 MB | Adobe PDF | OPEN | None | View/Download |
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.