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Stabilization of Supramolecular Membrane Protein-Lipid Bilayer Assemblies Through Immobilization in a Crystalline Exoskeleton

preprint
revised on 08.01.2021, 14:59 and posted on 08.01.2021, 20:10 by Fabian C. Herbert, Sameera Abeyrathna, Nisansala Abeyrathna, Yalini Wijesundara, Olivia Brohlin, Francesco Carraro, Heinz Amenitsch, paolo falcaro, Michael A. Luzuriaga, Alejandra Durand-Silva, Shashini D. Diwakara, Ronald A. Smaldone, Gabriele Meloni, Jeremiah J. Gassensmith

Artificial native-like lipid bilayer systems constructed from phospholipids assembling into unilamellar liposomes allow the reconstitution of detergent-solubilized transmembrane proteins into supramolecular lipid-protein assemblies called proteoliposomes, which mimic cellular membranes. Stabilization of these complexes remains challenging because of their chemical composition, the hydrophobicity and structural instability of membrane proteins, and the lability of interactions between protein, detergent, and lipids within micelles and lipid bilayers. In this work we demonstrate that metastable lipid, protein-detergent, and protein-lipid supramolecular complexes can be successfully generated and immobilized within zeolitic-imidazole framework (ZIF) to enhance their stability against chemical and physical stressors. Upon immobilization in ZIF bio-composites, blank liposomes, and model transmembrane metal transporters in detergent micelles or embedded in proteoliposomes resist elevated temperatures, exposure to chemical denaturants, aging, and mechanical stresses. Extensive morphological and functional charac- terization of the assemblies upon exfoliation reveal that all these complexes encapsulated within the framework maintain their native morphology, structure, and activity, which is otherwise lost rapidly without immobilization.

Funding

CAREER: Viral Capsids as Smart Nanocontainers

Directorate for Mathematical & Physical Sciences

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Welch Foundation [AT-1989- 20190330]

Welch Foundation (Grant: AT-1935-20170325)

Principles of selectivity and translocation in transition metal transporter

National Institute of General Medical Sciences

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Army Research Laboratory (W911NF-18-2- 0035)

Collaborative Research: L-RNA Based Reactive Oxygen Species Detection and Response Systems

Directorate for Mathematical & Physical Sciences

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Precisely Oriented Porous Crystalline Films and Patterns

European Research Council

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History

Email Address of Submitting Author

gassensmith@utdallas.edu

Institution

The University of Texas at Dallas

Country

United States

ORCID For Submitting Author

0000-0001-6400-8106

Declaration of Conflict of Interest

none

Version Notes

version 2, the second version.

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