Abstract
Effects of anionic lipids and heparin on the conformation of plasma proteins, such as albumin, γ-globulin, and fibrinogen were investigated by evaluating both α-helix and β-structure contents from circular dichroism (CD) spectra. Sodium dodecyl sulfate and sodium dodecylbenzenesulfonate increased the α-helix content of γ-globulin, and β-structure content of fibrinogen accompanied with decreasing α-helix content, while they stepwise disrupted the α-helix of albumin with increasing their concentration. It was concluded that the hydrophobic interaction was predominant for binding albumin, while the electrostatic interaction affected the structural changes of γ-globulin more than hydrophobic interaction.
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