A general approach to protein folding using thermostable exoshells

Samira Sadeghi, Siddharth Deshpande, Girish Vallerinteavide Mavelli, Alphan Aksoyoglu, Jayesh Bafna, Mathias Winterhalter, R. Manjunatha Kini, David P. Lane and Chester L. Drum ()
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Samira Sadeghi: National University of Singapore
Siddharth Deshpande: National University of Singapore
Girish Vallerinteavide Mavelli: National University of Singapore
Alphan Aksoyoglu: Jacobs University Bremen
Jayesh Bafna: Jacobs University Bremen
Mathias Winterhalter: Jacobs University Bremen
R. Manjunatha Kini: National University of Singapore
David P. Lane: P53 Laboratory, Agency for Science, Technology and Research (A*STAR)
Chester L. Drum: National University of Singapore

Nature Communications, 2021, vol. 12, issue 1, 1-15

Abstract: Abstract In vitro protein folding is a complex process which often results in protein aggregation, low yields and low specific activity. Here we report the use of nanoscale exoshells (tES) to provide complementary nanoenvironments for the folding and release of 12 highly diverse protein substrates ranging from small protein toxins to human albumin, a dimeric protein (alkaline phosphatase), a trimeric ion channel (Omp2a) and the tetrameric tumor suppressor, p53. These proteins represent a unique diversity in size, volume, disulfide linkages, isoelectric point and multi versus monomeric nature of their functional units. Protein encapsulation within tES increased crude soluble yield (3-fold to >100-fold), functional yield (2-fold to >100-fold) and specific activity (3-fold to >100-fold) for all the proteins tested. The average soluble yield was 6.5 mg/100 mg of tES with charge complementation between the tES internal cavity and the protein substrate being the primary determinant of functional folding. Our results confirm the importance of nanoscale electrostatic effects and provide a solution for folding proteins in vitro.

Date: 2021
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DOI: 10.1038/s41467-021-25996-4

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