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Research Article

ECB. 2021; 10(3): 155-166


METHODS of INTEGRAL MEMBRANE PROTEIN EXTRACTION and THEIR LIMITATIONS

Kallakuri A., Rajapakse H.E.




Abstract

Membrane proteins makeup around one-third of all proteins in the body and play important roles in signal transduction, selective molecular transmission and membrane integrity. They also serve as important drug targets. Therefore, accurate structural and functional analysis of membrane proteins is critical. The extraction and study of membrane proteins is limited due to their amphipathic nature, making them difficult to solubilize in aqueous media. Integral membrane proteins can be extracted from bio-membranes with detergents and purified into detergent micelles, bicelles, bilayers, or other forms of amphipathic molecules. These platforms do not necessarily mimic bio-membranes and, therefore, may not reflect the integral membrane proteins' accurate biological structure and function. Recent studies have introduced better representations of the bio-membrane, such as membrane mimicking nanoparticles, lipid nanodiscs (LNDs) and their variations, and artificial polymers. Due to some limitations described below, there are continuous efforts to develop better platforms that correctly resemble plasma membranes, leading to the correct biological structure and function of membrane proteins for in vitro studies. This mini-review comprehensively summarizes the recent developments of membrane proteins extraction, their advantages and disadvantages.

Key words: Hydrophobic; Lipids; Membrane Protein; Structural Analysis; Transmembrane






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