Negatively charged food additive dye 'Allura Red' rapidly induces SDS-soluble amyloid fibril in beta-lactoglobulin protein
| Autor: | Nasser Abdulatif Al-Shabib, Ajamaluddin Malik, Abdulrahman M. Al-Senaidy, Rizwan Hasan Khan, Monis Bilal Shamsi, Mohammad A. Alsenaidy, Syed Hidayathulla, Fohad Mabood Husain, Javed Masood Khan |
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| Rok vydání: | 2018 |
| Předmět: |
Models
Molecular 0301 basic medicine Amyloid Lactoglobulins Protein aggregation Fibril Biochemistry Fluorescence Protein Structure Secondary Hydrophobic effect Protein Aggregates 03 medical and health sciences chemistry.chemical_compound Nephelometry and Turbidimetry Structural Biology Animals Scattering Radiation Molecular Biology Beta-lactoglobulin Gel electrophoresis Chromatography 030102 biochemistry & molecular biology biology Sodium Dodecyl Sulfate Congo Red General Medicine Protein Structure Tertiary Congo red Kinetics 030104 developmental biology Solubility chemistry Transmission electron microscopy Biophysics biology.protein Cattle Food Additives Azo Compounds |
| Zdroj: | International Journal of Biological Macromolecules. 107:1706-1716 |
| ISSN: | 0141-8130 |
| Popis: | Recent studies have led to an increased interest to categorize small molecular inhibitors of protein fibrillation. In this study, we used spectroscopy, microscopy and gel electrophoresis techniques that provides an elaborated description of the Allura Red-induced amyloid fibrillation in the β-LG protein at two pHs (7.4 and 3.5). The spectroscopy results show that β-LG protein form aggregates in the presence of Allura Red (0.04–15.0 mM) at pH 3.5 due to electrostatic and hydrophobic interactions. However, at pH 7.4, the β-LG does not interact electrostatically with Allura Red and therefore no aggregation occurred. The Allura Red-induced aggregates have an amyloid-like structure that was confirmed by far-UV CD, Congo Red and transmission electron microscopy (TEM). The CD spectrum of β-LG contains single minima at ∼218 nm, which shifts towards higher wavelength minima at ∼225 nm in the presence of Allura Red, characteristics of the cross β-sheet structure. The TEM results suggest that β-LG form long straight fibril when exposed to Allura Red at pH 3.5. The Allura Red-induced amyloid fibril is SDS-soluble confirmed by SDS-PAGE techniques. A far UV CD result shows the conversion of Allura Red induced cross β-sheet structure into alpha-helical structure in the presence of increasing concentration of SDS. The results of this study suggest that the electrostatic, as well as hydrophobic interactions play an important role during Allura Red-induced β-LG fibrillation. |
| Databáze: | OpenAIRE |
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