Surfactant-driven modifications in protein structure

The interaction between proteins and surfactants has gained significant research interest due to its extensive applications across various fields, including the food industry, cosmetics, and medicine. Surfactants are known to unfold the proteins, where there are extensive models describing the basic mechanism of such unfolding and the resultant structure formed across micro-to-macro length scales. These models grounded on extensive experimental and simulation studies aim to predict the interaction dynamics based on several physicochemical parameters, such as surfactant properties (e.g., ionic character and tail length), protein characteristics (e.g., charge and isoelectric point), and solution conditions (e.g., pH, ionic strength, and temperature). Recently, there has been growing interest in the refolding of surfactant-induced unfolded proteins using combinations of ionic and nonionic surfactants and some mechanical procedures such as dilution, dialysis, etc. While the mechanisms of such refolding are still being explored, a general consensus suggests preferential binding of ionic surfactants with nonionic surfactants to form mixed micelles, rather than protein–surfactant complexes. It has also been demonstrated that the interaction of proteins with surfactants can be effectively utilized to guide the heat-induced gelation of proteins. This review article will summarize the fundamentals and recent updates on (i) protein interaction with surfactants; (ii) the phenomenon of protein unfolding and refolding, and (iii) the utilization of protein–surfactant interactions to direct heat-induced protein gelation.