Interaction between bovine serum albumin and equimolarly mixed cationic–anionic surfactants decyltriethylammonium bromide–sodium decyl sulfonate

Hydrophobization of bovine serum albumin with cationic surfactants with different hydrophobic chain length

“…Considering the necklace model, it can be established from the insert in Fig. 2 [43], which establish the relevance of this model.…”

Significant effect of polar head group of surfactants on the solubilization of Zein in mixed micellar (SDS–DDAB) media

“…In addition, the alkyl chain of the surfactant molecules interacts through hydrophobic bonding to the nonpolar parts present on the surface as well as in the interior of the globular proteins. The unfolding of the protein is believed to occur beyond the saturation of the protein by the surfactants [8][9][10].…”

Role of surfactant on the proteolysis of aqueous bovine serum albumin

“…BSA is often used in studies of the interaction between proteins and surfactants (Gelamo et al, 2002;Lu et al, 2005;Valstar et al, 2000Valstar et al, , 2001. Its primary structure is characterized by low tryptophan content and by high content of cysteine that stabilizes nine loops, and by charged amino acids, such as aspartic and glutamic acids, lysine, and arginine (Brown and Shockley, 1982).…”

“…For example, compact protein substrates tend to resist proteolysis, whereas unfolded or partially unfolded proteins are generally more susceptible to proteolytic degradation (Daniel et al, 1982;Markert et al, 2001). The protein bovine serum albumin (BSA) studied here, interacts with a number of surfactants including alkyl sulfates, alkyl sulfonates, and trimethylammonium bromides (Kaneshina et al, 1973;Reynolds et al, 1967) to induce conformational change (Gelamo and Tabak, 2000;Lu et al, 2005Lu et al, , 2006. Likewise, partial unfolding of enzymes due to surfactant generally results in loss of enzymatic activity (Cruzten and Douglas, 1999;Stoner et al, 2004).…”