Next Article in Journal / Special Issue
Comparing the Recombinant Protein Production Potential of Planktonic and Biofilm Cells
Previous Article in Journal
The Genus Wallemia—From Contamination of Food to Health Threat
Previous Article in Special Issue
Genetic Tools and Techniques for Recombinant Expression in Thermophilic Bacillaceae
Article Menu
Issue 2 (June) cover image

Export Article

Open AccessReview
Microorganisms 2018, 6(2), 47; https://doi.org/10.3390/microorganisms6020047

Polyionic Tags as Enhancers of Protein Solubility in Recombinant Protein Expression

Division of Molecular Therapeutics and Formulation, School of Pharmacy, University of Nottingham, Nottingham NG7 2RD, UK
*
Author to whom correspondence should be addressed.
Received: 9 April 2018 / Revised: 16 May 2018 / Accepted: 21 May 2018 / Published: 23 May 2018
(This article belongs to the Special Issue Recombinant Protein Expression in Microorganisms)
Full-Text   |   PDF [1346 KB, uploaded 23 May 2018]   |  

Abstract

Since the introduction of recombinant protein expression in the second half of the 1970s, the growth of the biopharmaceutical field has been rapid and protein therapeutics has come to the foreground. Biophysical and structural characterisation of recombinant proteins is the essential prerequisite for their successful development and commercialisation as therapeutics. Despite the challenges, including low protein solubility and inclusion body formation, prokaryotic host systems and particularly Escherichia coli, remain the system of choice for the initial attempt of production of previously unexpressed proteins. Several different approaches have been adopted, including optimisation of growth conditions, expression in the periplasmic space of the bacterial host or co-expression of molecular chaperones, to assist correct protein folding. A very commonly employed approach is also the use of protein fusion tags that enhance protein solubility. Here, a range of experimentally tested peptide tags, which present specific advantages compared to protein fusion tags and the concluding remarks of these experiments are reviewed. Finally, a concept to design solubility-enhancing peptide tags based on a protein’s pI is suggested. View Full-Text
Keywords: protein solubility; peptide tag; protein fusion tag; polycationic; polyanionic; recombinant protein expression protein solubility; peptide tag; protein fusion tag; polycationic; polyanionic; recombinant protein expression
Figures

Figure 1

This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).
SciFeed

Share & Cite This Article

MDPI and ACS Style

Paraskevopoulou, V.; Falcone, F.H. Polyionic Tags as Enhancers of Protein Solubility in Recombinant Protein Expression. Microorganisms 2018, 6, 47.

Show more citation formats Show less citations formats

Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Related Articles

Article Metrics

Article Access Statistics

1

Comments

[Return to top]
Microorganisms EISSN 2076-2607 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top