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Biochem Soc Trans. 2017 Feb 8;45(1):15-26. doi: 10.1042/BST20160019.

Durable vesicles for reconstitution of membrane proteins in biotechnology.

Author information

1
School of Chemistry and Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds LS2 9JT, U.K. p.a.beales@leeds.ac.uk.
2
School of Chemistry and Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds LS2 9JT, U.K.
3
School of Biomedical Sciences and Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds LS2 9JT, U.K.

Abstract

The application of membrane proteins in biotechnology requires robust, durable reconstitution systems that enhance their stability and support their functionality in a range of working environments. Vesicular architectures are highly desirable to provide the compartmentalisation to utilise the functional transmembrane transport and signalling properties of membrane proteins. Proteoliposomes provide a native-like membrane environment to support membrane protein function, but can lack the required chemical and physical stability. Amphiphilic block copolymers can also self-assemble into polymersomes: tough vesicles with improved stability compared with liposomes. This review discusses the reconstitution of membrane proteins into polymersomes and the more recent development of hybrid vesicles, which blend the robust nature of block copolymers with the biofunctionality of lipids. These novel synthetic vesicles hold great promise for enabling membrane proteins within biotechnologies by supporting their enhanced in vitro performance and could also contribute to fundamental biochemical and biophysical research by improving the stability of membrane proteins that are challenging to work with.

KEYWORDS:

bionanotechnology; block copolymers; in vitro reconstitution; membrane proteins; synthetic biology; vesicles

PMID:
28202656
PMCID:
PMC5310719
DOI:
10.1042/BST20160019
[Indexed for MEDLINE]
Free PMC Article

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