Protective Effects of Small Amounts of Bis(2-ethylhexyl)sulfosuccinate on the Helical Structures of Human and Bovine Serum Albumins in Their Thermal Denaturations

• Published in: Langmuir Vol. 21; no. 12; pp. 5524 - 5528
• Main Authors: Moriyama, Yoshiko, Takeda, Kunio
• Format: Journal Article
• Language: English
• Published: Washington, DC American Chemical Society 07.06.2005
• Subjects: Animals; Cattle; Chemistry; Colloidal state and disperse state; Diethylhexyl Phthalate - chemistry; Exact sciences and technology; General and physical chemistry; Hot Temperature; Humans; Micelles. Thin films; Protein Denaturation; Protein Renaturation; Protein Structure, Secondary; Serum Albumin - chemistry; Serum Albumin, Bovine - chemistry; Human; Bovine; Rod; Denaturation; Albumin; Micelle; Ions; Serum albumin; Surfactant; Ionic surfactant; Protein; Circular dichroism; Anionic surfactant; Vertebrata; Mammalia; Sodium; Residue; Helical structure; Artiodactyla; Aggregate; Aerosol OT; Monomer; Protection; Ungulata
• ISSN: 0743-7463; 1520-5827
• DOI: 10.1021/la050252j

The protective effect of an anionic double-tailed surfactant, sodium bis(2-ethylhexyl)sulfosuccinate (AOT), on the structures of human serum albumin (HSA) and bovine serum albumin (BSA) in their thermal denaturations was examined by means of circular dichroism measurements. The structural changes of these albumins were reversible in the thermal denaturation below 50 °C, but became partially irreversible above this temperature. The effect was observed in the thermal denaturation above 50 °C. Although the helicity of HSA decreased from 66% to 44% at 65 °C in the absence of the surfactant, the decrement of it was restrained in the coexistence of AOT of extremely low concentrations. When the HSA concentration was 10 μM, the maximal protective effect appeared at 0.15 mM AOT. In the coexistence of the surfactant of this concentration, the helicity was maintained at 58% at 65 °C, increasing to the original value upon cooling to 25 °C. Beyond 0.15 mM AOT, the helicity sharply decreased until 3 mM AOT. A particular AOT concentration required to induce the maximal protective effect ([AOT]REQ) was examined at different HSA concentrations. [AOT]REQ shifted to higher values with an increase of the protein concentration. From the protein concentration dependences of [AOT]REQ, the maximal protection was estimated to require 8.0 and 5.0 AOT ions per a molecule of HSA and BSA, respectively. The AOT concentration, where the protective effect was observed, was too low to form its micelle-like aggregate. Then the protein structures might be stabilized by a cross-linking of surfactant monomers bound to specific sites. These specific sites might exist between a group of nonpolar residues and a positively charged residue located on several sets of amphiphilic helical rods in the proteins. Such a unique function of the double-tailed ionic surfactant is first presented by its characteristic nature as an amphiphilic material.