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
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