Membrane Proteins Solubilization and Stabilization

Many of the difficulties associated with membrane proteins structure, function and drug discovery have stemmed from the need to solubilize and stabilize membrane proteins from the membrane into aqueous environment. This is because membrane proteins in their native state display large hydrophobic surfaces, which are incompatible with the aqueous environment. Solubilization and stabilization of membrane proteins is a critical step that represents the main obstacle for membrane proteins biochemistry and structural biology. Therefore, the development of effective membrane protein solubilization and stabilization tools is essential to unlock the structural and functional details of membrane proteins, and to develop new drugs ^[1].

Alfa Chemistry has developed diverse strategies for solubilization of membrane proteins from membranes and for maintenance of these proteins in a native-like state in aqueous solution.

Our Strategies

Our membrane proteins solubilization and stabilization service includes four different strategies that you to choose from. Each methods can mimic the original membrane of the target membrane proteins and make them solubilize and stabilize in an aqueous solution, which can retain functions and structure of membrane proteins after natural membrane removed.

Membrane proteins in detergents

Detergent mediated solubilization and stabilization of membrane proteins remains the canonical and conventional approach prior to biochemical investigation. Selecting suitable detergents for the solubilization and stabilization of a specific membrane proteins is very crucial. Of course, Alfa Chemistry will perform an exhaustive approach to identify the optimal detergent, balancing both solubilization efficacy and protein stability for each individual protein.

Fig. 1. Schematic representation of solubilization and stabilization of membrane proteins in detergents.

Membrane proteins in lipid containing systems

Lipid containing systems are one of the most frequently used methods for stabilizing membrane proteins. At Alfa Chemistry, detergent-extracted membrane proteins can be reconstituted into lipids containing systems such as mixed micelles, planar bilayers or liposomes, which can be used in the functional investigations of membrane proteins transporters or indeed the reconstitution of entire transport systems.

Membrane proteins in nanodiscs

Nanodiscs constitute a discoidal phospholipid bilayer section stabilized by either an amphipathic protein, peptide or polymer, which act to shroud the hydrophobic phospholipid tails from the aqueous environment. Membrane scaffold proteins (MSP) nanodiscs and polymer-based nanodiscs (styrene maleic acid (SMA) and diisobutylene maleic acid (DIBMA)) technologies are available in Alfa Chemistry to solubilize and stabilize membrane proteins. MSP nanodiscs can create a perfect replication of the native membrane environment of the membrane proteins. And polymer-based nanodiscs can directly extract proteins from the membrane without destroying lipids that are beneficial to the structure and function of organism.

Fig. 2. Schematic representation of solubilization and stabilization of membrane proteins in (A) MSP nanodiscs and (B) polymer nanodiscs.

Membrane proteins in amphipols

Amphipols are short amphipathic polymers that self-assemble to conceal hydrophobic membrane proteins portions, maintaining their solubility in aqueous solutions. Amphipols are understood to be mild detergents that may promote stabilization of membrane proteins and make them subsist in a more natural, stable state. Years of unmatched experience made Alfa Chemistry the perfect choice for this project.

Fig. 3. Schematic representation of solubilization and stabilization of membrane proteins in amphipols.

Order Process

References

1. Ratkeviciute G., et al. Methods for the solubilisation of membrane proteins: the micelle-aneous world of membrane protein solubilisation[J]. Biochemical Society Transactions, 2021, 49(4): 1763-1777.

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