How Do Detergents Solubilize Proteins?


The structure of detergents is key to its ability to function as a solubilization agent. Detergent molecules contain a polar head group from which extends a long hydrophobic carbon tail.

The amphipathic properties of the detergent molecules allows them to exhibit unique properties in aqueous solutions. The polar (hydrophilic) head groups interact with the hydrogen bonds of the water molecules and the hydrophobic tails aggregate resulting in highly organized spherical structures called micelles. At low concentrations, the detergents exist as single molecules or small aggregates and as the concentration increases micelles begin to form.


A wide range of detergents are routinely used to release, or solubilize, proteins from lipid membranes. 
Biological membranes consist of phospholipids that are similar to detergents as they have the same amphipathic properties. The phospholipids have a charged polar head normally connected to two hydrophobic groups or tails. The phospholipids assemble as bilayers, with the hydrophobic tails between two faces of polar head groups.

For biological membranes , proteins and lipids (i.e. cholesterol) are embedded in the bilayer forming the fluid mosaic model. The proteins are held in the lipid bilayer by hydrophobic interations between the lipid tails and hydrophobic protein domains. These integral membrane proteins are not soluble in aqueous solutions as they aggregate to protect their hydrophobic domains, but are soluble in detergent solutions.