Unraveling the molecular mechanism of the effects of sodium dodecyl sulfate, salts, and sugars on amyloid fibril formation in camel IgG

Ismael, Mohamad Alhasan; Khan, Javed Masood; Malik, Ajamaluddin; Alsenaidy, Mohammad A.; Hidayathulla, Syed; Khan, Rizwan Hasan; Sen, Priyankar; Irfan, Mohammad; Al-Senaidy, Abdulrahman M.

doi:10.1016/j.colsurfb.2018.06.035

Cited by 28 publications

(6 citation statements)

References 44 publications

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“…In addition, PP29 and PP30 are the most hydrophobic compounds of the tested library (Table S1) and they could favor protein aggregation by dispersing the water structure around the Aβ peptide. A similar effect was reported for the hydrophobic tail of SDS, which is able to make contacts with hydrophobic protein stretches repelling the water molecules wrapped around the protein thus perturbing protein/solvent interactions and inducing aggregation …”

Section: Resultssupporting

confidence: 68%

Biophysical and in Vivo Studies Identify a New Natural-Based Polyphenol, Counteracting Aβ Oligomerization in Vitro and Aβ Oligomer-Mediated Memory Impairment and Neuroinflammation in an Acute Mouse Model of Alzheimer’s Disease

Tomaselli

Vitola

Pagano

et al. 2019

ACS Chem. Neurosci.

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In this study natural-based complex polyphenols, obtained through a smart synthetic approach, have been evaluated for their ability to inhibit the formation of Aβ42 oligomers, the most toxic species causing synaptic dysfunction, neuroinflammation, and neuronal death leading to the onset and progression of Alzheimer’s disease. In vitro neurotoxicity tests on primary hippocampal neurons have been employed to select nontoxic candidates. Solution NMR and molecular docking studies have been performed to clarify the interaction mechanism of Aβ42 with the synthesized polyphenol derivatives, and highlight the sterical and chemical requirements important for their antiaggregating activity. NMR results indicated that the selected polyphenolic compounds target Aβ42 oligomeric species. Combined NMR and docking studies indicated that the Aβ42 central hydrophobic core, namely, the 17–31 region, is the main interaction site. The length of the peptidomimetic scaffold and the presence of a guaiacol moiety were identified as important requirements for the antiaggregating activity. In vivo experiments on an Aβ42 oligomer-induced acute mouse model highlighted that the most promising polyphenolic derivative (PP04) inhibits detrimental effects of Aβ42 oligomers on memory and glial cell activation. NMR kinetic studies showed that PP04 is endowed with the chemical features of true inhibitors, strongly affecting both the Aβ42 nucleation and growth rates, thus representing a promising candidate to be further developed into an effective drug against neurodegenerative diseases of the amyloid type.

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Section: Resultssupporting

confidence: 68%

Biophysical and in Vivo Studies Identify a New Natural-Based Polyphenol, Counteracting Aβ Oligomerization in Vitro and Aβ Oligomer-Mediated Memory Impairment and Neuroinflammation in an Acute Mouse Model of Alzheimer’s Disease

Tomaselli

Vitola

Pagano

et al. 2019

ACS Chem. Neurosci.

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“…27 Ismael et al recently found that SDS can induce amyloid fibrillation of IgG at lower concentrations and inhibit protein aggregation at higher concentrations. 41 In addition, SDS is a well-known surfactant which is able to promote the formation of amyloidbeta oligomer, an intermediate cytotoxic structure during amyloid fibrillation. 34 As for TX-100, a very recent study showed that the effect of TX-100 on the amyloid fibrillation of insulin was concentration-dependent.…”

Section: ■ Introductionmentioning

confidence: 99%

“…Mukhija et al recently investigated the effect of SDS on the amyloid fibrillation of human serum albumin (HSA) under physiological conditions and found that the micelle form of SDS could not only inhibit the HSA fibrillation process but also effectively disintegrate HSA fibrils . Ismael et al recently found that SDS can induce amyloid fibrillation of IgG at lower concentrations and inhibit protein aggregation at higher concentrations . In addition, SDS is a well-known surfactant which is able to promote the formation of amyloid-beta oligomer, an intermediate cytotoxic structure during amyloid fibrillation .…”

Section: Introductionmentioning

confidence: 99%

Modulation of Surface-Catalyzed Secondary Nucleation during Amyloid Fibrillation of Hen Egg White Lysozyme by Two Common Surfactants

et al. 2019

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Amyloid fibrillation by hen egg white lysozyme (HEWL) under the influences of two common surfactants, sodium dodecyl sulfate (SDS) and Triton X-100 (TX-100), was investigated with atomic force microscopy (AFM) and Fourier transform infrared (FTIR) spectroscopy. Detailed AFM investigations indicated that both SDS and TX-100 were able to induce some significant morphological changes of HEWL amyloid fibrils. Both SDS and TX-100 could induce a morphological change which was characterized with alternating fibril regions with increased thicknesses along the fibril axis. In addition, TX-100 was also able to induce a morphological change which was characterized with fibril branching. In contrast, the positively charged cetyltrimethylammonium bromide displayed no such effect as compared with the negatively charged SDS and the nonionic TX-100. These intriguing modulation effects of SDS and TX-100 on amyloid fibrillation were hypothesized to be due to surfactant-induced surface-catalyzed secondary nucleation owing to the noncovalent interaction between the surfactants and HEWL. The proposed hypothesis was further supported by FTIR spectroscopic investigation, which demonstrated the formation of a SDS−amyloid fibril complex and TX-100−amyloid fibril complex. Detailed FTIR analysis suggested that the tail group of SDS associated with amyloid fibrils is more disordered similar to that of SDS in aqueous solution, while the headgroup of SDS appears to interact with amyloid fibrils strongly similar to that of SDS in the solid state, and the ether groups of TX-100 associated with amyloid fibrils experienced a different microenvironment as compared with that of neat TX-100. Additional control experiments with FTIR spectroscopy revealed that the interactions of SDS/TX-100 with HEWL amyloid fibrils were different from those of SDS/TX-100 with HEWL amorphous aggregates. In addition, the β-sheet structures of the HEWL amyloid fibrils were found to be increased due to the influences of SDS and TX-100. Our work provides new insight into the modulation effects of surfactants on amyloid fibrillation.

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“…Similarly, when 5 mM DTT‐treated HEWL was incubated at pH 7.4 and 37°C without shaking for 5 h, it lost almost all of its secondary structure and no further structural conversion occurred over the next 7 days of incubation (Table 2; Figure 4A,B). When proteins denature and convert to amyloid, they frequently gain ellipticity between 215 and 230 nm, indicating the formation of amyloid‐like β‐sheet structures 44,45 . These results showed that the denatured HEWL under agitation or non‐agitation formed amorphous aggregates.…”

Section: Resultsmentioning

confidence: 90%

Agitation does not induce fibrillation in reduced hen egg‐white lysozyme at physiological temperature and pH

Malik

Khan

Alhomida

et al. 2023

J of Molecular Recognition

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Several proteins and peptides tend to form an amyloid fibril, causing a range of unrelated diseases, from neurodegenerative to certain types of cancer. In the native state, these proteins are folded and soluble. However, these proteins acquired β‐sheet amyloid fibril due to unfolding and aggregation. The conversion mechanism from well‐folded soluble into amorphous or amyloid fibril is not well understood yet. Here, we induced unfolding and aggregation of hen egg‐white lysozyme (HEWL) by reducing agent dithiothreitol and applied mechanical sheering force by constant shaking (1000 rpm) on the thermostat for 7 days. Our turbidity results showed that reduced HEWL rapidly formed aggregates, and a plateau was attained in nearly 5 h of incubation in both shaking and non‐shaking conditions. The turbidity was lower in the shaking condition than in the non‐shaking condition. The thioflavin T binding and transmission electron micrographs showed that reduced HEWL formed amorphous aggregates in both conditions. Far‐UV circular dichroism results showed that reduced HEWL lost nearly all alpha‐helical structure, and β‐sheet secondary structure was not formed in both conditions. All the spectroscopic and microscopic results showed that reduced HEWL formed amorphous aggregates under both conditions.

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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

Cited by 28 publications

References 44 publications

Biophysical and in Vivo Studies Identify a New Natural-Based Polyphenol, Counteracting Aβ Oligomerization in Vitro and Aβ Oligomer-Mediated Memory Impairment and Neuroinflammation in an Acute Mouse Model of Alzheimer’s Disease

Biophysical and in Vivo Studies Identify a New Natural-Based Polyphenol, Counteracting Aβ Oligomerization in Vitro and Aβ Oligomer-Mediated Memory Impairment and Neuroinflammation in an Acute Mouse Model of Alzheimer’s Disease

Modulation of Surface-Catalyzed Secondary Nucleation during Amyloid Fibrillation of Hen Egg White Lysozyme by Two Common Surfactants

Agitation does not induce fibrillation in reduced hen egg‐white lysozyme at physiological temperature and pH

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