I was doing the purification of Human Hsp40, and many papers refer to use detergent during the purification protocol. I just wanted to know how the detergent Triton-X or Brij-58 helps in avoiding the formation of oligomers.
Proteins can aggregate if they have exposed hydrophobic surfaces or are just hydrophobic overall. By coating those surfaces, detergents can prevent the aggregation. The detergent concentration may not have to be very high to achieve this, since only a few detergent molecules per protein may be sufficient.
For very hydrophobic proteins, such as membrane proteins, detergents are required just to keep the proteins in solution. In that situation, the concentration of the detergent must be high enough to form micelles, preferably high enough that each micelle contains a single protein molecule.
How much or what concentration is something that you need to determine experimentally. Start with mild detergents (uncharged). High concentrations will denature the protein.
Triton X-100 and Brij-58 are non-ionic detergents with uncharged hydrophilic headgroups and are considered as mild surfactants that break protein-lipid and lipid-lipid interactions, but typically not protein-protein interactions, and generally, they do not denature proteins. Therefore, many membrane proteins may be solubilized in their native and active form, retaining their protein interacting partners.
For more clear scenerio about this topic you can read this article
Omar Gonzalez-Ortega The concentration I get around is close to 100 micro molar. I recently tried the purification with a 0.1% Triton-X solution in all my purification buffers. Since my protein has 10 cysteines in it, I don't know how much did this detergent addition helped in preventing aggregation.