Aquaporins:Expression, purification and characterization


Aquaporin water channels facilitate the bi-directional flow of water and small, neutral solutes down an osmotic gradient in all kingdoms of life. Over the last two decades, the availability of high-quality protein has underpinned progress in the structural and functional characterization of these water channels. In particular, recombinant protein technology has guaranteed the supply of aquaporin samples that were of sufficient quality and quantity for further study. Here we review the features of successful expression, purification and characterization strategies that have underpinned these successes and that will drive further breakthroughs in the field. Overall, Escherichia coli is a suitable host for prokaryotic isoforms, while Pichia pastoris is the most commonly-used recombinant host for eukaryotic variants. Generally, a two-step purification procedure is suitable after solubilization in glucopyranosides and most structures are determined by X-ray following crystallization.

Publication DOI:
Divisions: College of Health & Life Sciences > School of Biosciences
College of Health & Life Sciences > School of Biosciences > Cellular and Molecular Biomedicine
College of Health & Life Sciences
Additional Information: © 2021, Elsevier. Licensed under the Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International Funding: The work presented in this study was supported by research grants from the Swedish research Council; VR-M, Structural studies of aquaporin:protein complexes as well as VR-RÅC (2017-06727), and the Swedish Brain Foundation (FO2018-0231) to Kristina Hedfalk and from the Biotechnology & Biological Sciences Research Council (through BB/P025927/1) to Roslyn M. Bill.
Uncontrolled Keywords: Aquaporin,Proteoliposomes,Recombinant production,Water channel,Biophysics,Biochemistry,Cell Biology
Publication ISSN: 1879-2642
Last Modified: 09 Jul 2024 07:40
Date Deposited: 07 Jun 2021 09:01
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Related URLs: https://www.sci ... 1000?via%3Dihub (Publisher URL)
http://www.scop ... tnerID=8YFLogxK (Scopus URL)
PURE Output Type: Article
Published Date: 2021-09-01
Published Online Date: 2021-05-18
Accepted Date: 2021-05-12
Authors: Bill, Roslyn M (ORCID Profile 0000-0003-1331-0852)
Hedfalk, Kristina

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