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Unraveling the molecular mechanism of the effects of sodium dodecyl sulfate, salts, and sugars on amyloid fibril formation in camel IgG
Ismael M.A, Khan J.M, Malik A, Alsenaidy M.A, Hidayathulla S, Khan R.H, Irfan M, Alsenaidy A.M.,
Published in Elsevier BV
PMID: 29957532
Volume: 170
Pages: 430 - 437
Sodium dodecyl sulfate (SDS) is an anionic surfactant that can be used to stimulate protein fibrillation in vitro. Here, we investigated the effects of SDS on camel IgG aggregation at pH 3.5 and 7.4. SDS-induced amyloid fibril formation in camel IgG was examined by turbidity measurements, Rayleigh scattering, Thioflavin T (ThT) fluorescence, intrinsic fluorescence, circular dichroism (CD), and transmission electron microscopy (TEM). The results suggest that low SDS concentrations (0.2–2.0 mM) induce amyloid-like aggregates of camel IgG at pH 3.5, indicating an SDS/camel IgG ratio below 1000. However, in the presence of higher concentrations of SDS (2.5–10.0 mM), amyloid fibril formation was not observed. Furthermore, at the higher concentrations, the β-sheet structure of camel IgG was transformed into a α-helical structure. The amyloid fibril formation was not observed in the presence of SDS at pH 7.4. Additionally, the role of salts and sugars was evaluated in the SDS-induced aggregation process. Interestingly, in the presence of 0.15 N of NaCl and (NH4)2SO4, SDS promoted camel IgG aggregation up to very high concentrations of SDS (0.2–10.0 mM; SDS/camel IgG ratio, 95–4750) and no suppression was observed. Moreover, osmoprotectants (trehalose and sucrose) were ineffective, neither promoting nor inhibiting the SDS-induced aggregation process. However, at pH 3.5, electrostatic and hydrophobic interactions, and hydrogen bonds were the major contributing factors in SDS-induced fibrillation. However, no aggregation was observed at pH 7.4 due to electrostatic repulsion between SDS and camel IgG because both of these molecules have overall similar charges. © 2018 Elsevier B.V.
About the journal
JournalData powered by TypesetColloids and Surfaces B: Biointerfaces
PublisherData powered by TypesetElsevier BV
Open Access0