Current affinity approaches for purification of recombinant proteins

Abstract

Recombinant proteins have wide applications in the development of pharmaceutical compounds, industrial applications of enzymes, and basic proteomics research. In this way, efficient production of recombinant proteins with high purity needs efficient purification methods. Various strategies have been devised to improve these proteins purification such as affinity purification and physicochemical purification methods which the affinity purification has some advantages over the others. Affinity strategies especially fusion strategies have been devised as indispensable tools for the massive parallel production, identification and purification of recombinant proteins from the host systems. These strategies facilitate commercial and industrial formulations of recombinant proteins, improve the study of protein interactions at the molecular level, and develop highly sensitive and specific bioassays. Recently, various surface-modified nanoparticles have been widely developed to enhance recovery and purification of recombinant proteins such as Hydrophobic polymer nanoparticles and Oleosin nanoparticles. In this review, we aim to discuss affinity purification technologies and address the principles, advantages, limitations and potential applications of them.

Keywords:

• recombinant protein
• affinity purification
• fusion purification

PUBLIC INTEREST STATEMENT

Purification is an essential part of developing protein-based products. The detailed knowledge of protein purification methods is required for researchers of molecular biology and biochemistry field to well tune the most suitable strategy for purification of their protein of interest from protein factories. Therefore, in this scientific article, we have reviewed the most popular methods for purification of recombinant proteins.

Competing Interests

The authors declare no competing interests.

Acknowledgements

This article has been extracted from the MSc thesis number “95/2-2/1”. The authors would like to thank the Research Deputy of Tabriz University of Medical Sciences for their financial support.

Conflict of Interest

The authors declare no conflict of interest.

Cover Image

Source:

Additional information

Funding

This work was supported by the Research Deputy of Tabriz University of Medical Sciences [95/2-2/1].

Notes on contributors

Sahar Mahmoodi

Sahar Mahmoodi has worked on the development of visual strip test for point of care detection of recombinant proteins.

 Mohammad Pourhassan-Moghaddam is currently focusing on the preparation of bio and nanomaterials, including recombinant proteins, for application in the fields of cellular and molecular diagnostics.

 David W. Wood is known for groundbreaking research in self-cleaving affinity tag technology for the purification of recombinant proteins. Current applications include new ways to purify recombinant proteins, bacterial biosensors that incorporate human drug targets, and new capabilities in drug discovery and drug delivery

 Hasan Majdi has worked on the development of SPR-based biosensors for detection of different proteins, including recombinant proteins.

 Nosratollah Zarghami’s group is working on targeting cancer cells using various materials. Recently, his group is focused on the development of recombinant coagulases for targeting tumour vascularisation.