Efficient protein renaturation using tunable hemifluorinated anionic surfactants as additives

Area of Science:

• Biochemistry
• Protein Chemistry
• Surfactant Science

Background:

• Protein denaturation can be caused by thermal or chemical agents.
• Renaturation of denatured proteins is crucial for biological activity.
• Surfactants are known to affect protein structure and stability.

Purpose of the Study:

• To investigate the efficacy of hemifluorinated anionic surfactants as renaturing additives.
• To determine the optimal concentration range for surfactant-assisted protein refolding.
• To evaluate the refolding yields of denatured bovine carbonic anhydrase (CAB).

Main Methods:

• Hemifluorinated anionic surfactants were used as additives.
• Bovine carbonic anhydrase (CAB) was thermally and chemically denatured.
• Protein refolding was assessed below the critical micelle concentration (CMC) of the surfactants.
• Refolding yields were quantified.

Main Results:

• Hemifluorinated anionic surfactants demonstrated effectiveness in protein renaturation.
• High refolding yields were achieved for denatured CAB.
• The renaturing effect was observed below the critical micelle concentration (CMC).

Conclusions:

• Hemifluorinated anionic surfactants are efficient renaturing agents for bovine carbonic anhydrase (CAB).
• The study highlights the potential of these surfactants for protein refolding applications.
• Optimal refolding occurs at surfactant concentrations below the CMC.