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Thermostable exoshells fold and stabilize recombinant proteins

Author

Listed:
  • Siddharth Deshpande

    (National University of Singapore
    National University of Singapore
    National University of Singapore)

  • Nihar D. Masurkar

    (National University of Singapore
    National University of Singapore)

  • Vallerinteavide Mavelli Girish

    (National University of Singapore
    National University of Singapore)

  • Malan Desai

    (National University of Singapore
    National University of Singapore)

  • Goutam Chakraborty

    (National University of Singapore
    National University of Singapore)

  • Juliana M. Chan

    (Nanyang Technological University
    Nanyang Technological University)

  • Chester L. Drum

    (National University of Singapore
    National University of Singapore
    Translational Laboratory in Genetic Medicine
    National University of Singapore)

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.

Suggested Citation

  • Siddharth Deshpande & Nihar D. Masurkar & Vallerinteavide Mavelli Girish & Malan Desai & Goutam Chakraborty & Juliana M. Chan & Chester L. Drum, 2017. "Thermostable exoshells fold and stabilize recombinant proteins," Nature Communications, Nature, vol. 8(1), pages 1-8, December.
    • Handle: RePEc:nat:natcom:v:8:y:2017:i:1:d:10.1038_s41467-017-01585-2
    DOI: 10.1038/s41467-017-01585-2
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