title: Sodium dodecyl sulphate modulates the fibrillation of human serum albumin in a dose-dependent manner and impacts the PC12 cells retraction.
abstract: Protein aggregation is impacted by many factors including temperature, pH, and the presence of surfactants, electrolytes, and metal ions. The addition of sodium dodecyl sulphate (SDS) at different concentrations may play a significant role in the human serum albumin (HSA) fibrillation pathway. Here the heat induction of HSA fibrillation incubated with different concentrations of SDS was evaluated using a variety of techniques. These included ThT fluorescence, Congo red absorbance, circular dichroism, dynamic light scattering, and atomic force microscopy (AFM). To explore HSA surface properties, the surface tension of solutions was measured using Du Noüy Ring method tensiometry. In addition, the criteria of neurite outgrowth and complexity were monitored by exposing PC12 cells to different forms of HSA amyloid intermediates. ThT fluorescence kinetic studies indicated that SDS at low concentrations induced more fibrillation of HSA, while SDS at high concentrations inhibited the fibrillation of HSA. At higher SDS concentrations hydrophobic forces had a significant role whereas at lower SDS concentrations electrostatic forces were dominant. The cell culture studies demonstrated the significant impact of SDS concentration on HSA fibrillation and subsequent neuronal cell morphology. The HSA incubated with low concentrations of SDS inhibited neurite outgrowth and complexity of the PC12 cells, whereas high concentrations of SDS had lesser effect. Thus, SDS acts as a salt at lower concentrations, while at higher concentrations acts as a chaperon, with significant impact on fibrillation of HSA.
authors: Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran.
authors: Sina
authors: S
authors: Movaghati
authors: Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran; Center of Excellence in Biothermodynamics, University of Tehran, Tehran, Iran. Electronic address: moosavi@ut.ac.ir.
authors: Ali Akbar
authors: AA
authors: Moosavi-Movahedi
authors: Neuroscience Research Centre, Shahid Beheshti University of Medical Sciences, Tehran, Iran.
authors: Fariba
authors: F
authors: Khodagholi
authors: Neuroscience Research Centre, Shahid Beheshti University of Medical Sciences, Tehran, Iran.
authors: Hadi
authors: H
authors: Digaleh
authors: Institute of Biochemistry and Biophysics, University of Tehran, Tehran, Iran.
authors: Ehsan
authors: E
authors: Kachooei
authors: Departments of Ophthalmology and Visual Sciences, and Biomedical Engineering, University of Wisconsin School of Medicine and Public Health, Madison, WI, USA.
authors: Nader
authors: N
authors: Sheibani
mesh_terms: D000818:Animals; D002942:Circular Dichroism; D004305:Dose-Response Relationship, Drug; D005453:Fluorescence; D006801:Humans; D007700:Kinetics; D018625:Microscopy, Atomic Force; D016716:PC12 Cells; D051381:Rats; D012709:Serum Albumin / Q000378:metabolism*; D012967:Sodium Dodecyl Sulfate / Q000494:pharmacology*; D013500:Surface Tension
chemical_list: D012709:Serum Albumin; D012967:Sodium Dodecyl Sulfate
keywords: Fibrillation; Human serum albumin; Neuron-like PC12 cells; Sodium dodecyl sulphate; Surface tension