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.
journal_name
Nat Communjournal_title
Nature communicationsauthors
Deshpande S,Masurkar ND,Girish VM,Desai M,Chakraborty G,Chan JM,Drum CLdoi
10.1038/s41467-017-01585-2subject
Has Abstractpub_date
2017-11-13 00:00:00pages
1442issue
1issn
2041-1723pii
10.1038/s41467-017-01585-2journal_volume
8pub_type
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