title: Fibrinogen stability under surfactant interaction.
abstract: Differential scanning calorimetry (DSC), circular dichroism (CD), difference spectroscopy (UV-vis), Raman spectroscopy, and small-angle X-ray scattering (SAXS) measurements have been performed in the present work to provide a quantitatively comprehensive physicochemical description of the complexation between bovine fibrinogen and the sodium perfluorooctanoate, sodium octanoate, and sodium dodecanoate in glycine buffer (pH 8.5). It has been found that sodium octanoate and dodecanoate act as fibrinogen destabilizer. Meanwhile, sodium perfluorooctanoate acts as a structure stabilizer at low molar concentration and as a destabilizer at high molar concentration. Fibrinogen's secondary structure is affected by all three studied surfactants (decrease in α-helix and an increase in β-sheet content) to a different extent. DSC and UV-vis revealed the existence of intermediate states in the thermal unfolding process of fibrinogen. In addition, SAXS data analysis showed that pure fibrinogen adopts a paired-dimer structure in solution. Such a structure is unaltered by sodium octanoate and perfluoroctanoate. However, interaction of sodium dodecanoate with the fibrinogen affects the protein conformation leading to a complex formation. Taken together, all results evidence that both surfactant hydrophobicity and tail length mediate the fibrinogen stability upon interaction.
authors: Soft Matter and Molecular Biophysics Group, Department of Applied Physics, University of Santiago de Compostela, Campus Vida s/n, 15782 Santiago de Compostela, Spain.
authors: Natalia
authors: N
authors: Hassan
authors: Leandro R S
authors: LR
authors: Barbosa
authors: Rosangela
authors: R
authors: Itri
authors: Juan M
authors: JM
authors: Ruso
mesh_terms: D000818:Animals; D002152:Calorimetry, Differential Scanning; D002210:Caprylates / Q000737:chemistry; D002417:Cattle; D002942:Circular Dichroism; D005340:Fibrinogen / Q000737:chemistry*; D005466:Fluorocarbons / Q000737:chemistry; D007850:Lauric Acids / Q000737:chemistry; D011489:Protein Denaturation; D055550:Protein Stability; D053838:Scattering, Small Angle; D013059:Spectrum Analysis, Raman; D013501:Surface-Active Agents / Q000737:chemistry*; D014961:X-Ray Diffraction
chemical_list: D002210:Caprylates; D005466:Fluorocarbons; D007850:Lauric Acids; D013501:Surface-Active Agents; C030358:lauric acid; D005340:Fibrinogen; C023036:perfluorooctanoic acid; C031492:octanoic acid