Effects of ionic and reductive atmosphere on the conformational rearrangement in hen egg white lysozyme prior to amyloid formation
| Autor: | Yuta Otsuka, Takahiro Kasai, Takashi Wada, Kazushi Komatsu, Yoshiko Minami, Tomoyo Sakaguchi, Satoru Goto, Tomoki Shiratori, Yohsuke Shimada |
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| Rok vydání: | 2019 |
| Předmět: |
Amyloid
education 02 engineering and technology Protein aggregation 01 natural sciences Dithiothreitol Protein Structure Secondary chemistry.chemical_compound Protein Aggregates Colloid and Surface Chemistry mental disorders 0103 physical sciences Animals Denaturation (biochemistry) Physical and Theoretical Chemistry Protein secondary structure 010304 chemical physics Chemistry Atmosphere Osmolar Concentration Surfaces and Interfaces General Medicine Hydrogen-Ion Concentration 021001 nanoscience & nanotechnology Isoelectric point Ionic strength Biophysics Muramidase Salts Lysozyme 0210 nano-technology Amyloid (mycology) Chickens Biotechnology |
| Zdroj: | Colloids and surfaces. B, Biointerfaces. 190 |
| ISSN: | 1873-4367 |
| Popis: | In this study, the combined effects of pH and salt concentration on the aggregation and amyloid formation of a charge-bearing protein (hen egg white lysozyme, HEWL) were investigated, as well as the inhibition of amyloid formation by using dithiothreitol (DTT) as a denaturing agent. Amyloid formation was found to depend on the ion strength and pH of the sample solution. Rather than the total charge, the partial charge of the amyloid related residues contributes to amyloid formation at pHisoelectric point (pI). On the other hand, at pHpI HEWL only undergoes alkaline denaturation regardless of the ionic strength. The effect of adding different amounts of DTT at different times on amyloid formation was also investigated. These results suggested that the positions of charges on a protein and the protein secondary structure are critical for protein aggregation and amyloid formation. |
| Databáze: | OpenAIRE |
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