Influence of the ionic strength on the amyloid fibrillogenesis of hen egg white lysozyme

Wawer, Jarosław; Szociński, Michał; Olszewski, Marcin; Piątek, Rafał; Naczk, M.; Krakowiak, Joanna

doi:10.1016/j.ijbiomac.2018.09.165

Cited by 42 publications

(16 citation statements)

References 38 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The striking feature of the K-peptide fibrils’ morphology is that the obtained amyloids are needle-like and stiff. The amyloids of the whole protein—hen egg white lysozyme—tend to be more curvy and elastic [ 23 , 35 ].…”

Section: Resultsmentioning

confidence: 99%

“…The results of spectroscopic methods must necessarily be confronted with imaging using microscopic techniques, such as transmission electron microscopy or atomic force microscopy (AFM). These measurements allows for detection of false negative results [ 23 ]. By applying all of the above-mentioned techniques, it is possible to obtain a comprehensive picture of fibrillation.…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Influence of Urea and Dimethyl Sulfoxide on K-Peptide Fibrillation

Wawer

Karczewski

Aranowski

et al. 2022

IJMS

Self Cite

View full text Add to dashboard Cite

Protein fibrillation leads to formation of amyloids—linear aggregates that are hallmarks of many serious diseases, including Alzheimer’s and Parkinson’s diseases. In this work, we investigate the fibrillation of a short peptide (K-peptide) from the amyloidogenic core of hen egg white lysozyme in the presence of dimethyl sulfoxide or urea. During the studies, a variety of spectroscopic methods were used: fluorescence spectroscopy and the Thioflavin T assay, circular dichroism, Fourier-transform infrared spectroscopy, optical density measurements, dynamic light scattering and intrinsic fluorescence. Additionally, the presence of amyloids was confirmed by atomic force microscopy. The obtained results show that the K-peptide is highly prone to form fibrillar aggregates. The measurements also confirm the weak impact of dimethyl sulfoxide on peptide fibrillation and distinct influence of urea. We believe that the K-peptide has higher amyloidogenic propensity than the whole protein, i.e., hen egg white lysozyme, most likely due to the lack of the first step of amyloidogenesis—partial unfolding of the native structure. Urea influences the second step of K-peptide amyloidogenesis, i.e., folding into amyloids.

show abstract

Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Influence of Urea and Dimethyl Sulfoxide on K-Peptide Fibrillation

Wawer

Karczewski

Aranowski

et al. 2022

IJMS

Self Cite

View full text Add to dashboard Cite

show abstract

“…The effect of fibrillation conditions on HEWL amyloidogenesis was tested on many occasions. Among others, the influences of temperature and pH [17], fibrillation in the presence of low molecular additives [18][19][20], impact of ionic strength [21], and shear or stirring rate [22,23] were examined. Investigations on peptide fibrillation have been much more limited.…”

Section: Introductionmentioning

confidence: 99%

DMSO and TMAO—Differences in Interactions in Aqueous Solutions of the K-Peptide

Godlewska

Cieśla

Wawer

et al. 2022

IJMS

Self Cite

View full text Add to dashboard Cite

Interactions between a solvent and their co-solute molecules in solutions of peptides are crucial for their stability and structure. The K-peptide is a synthetic fragment of a larger hen egg white lysozyme protein that is believed to be able to aggregate into amyloid structures. In this study, a complex experimental and theoretical approach is applied to study systems comprisingthe peptide, water, and two co-solutes: trimethylamide N-oxide (TMAO) or dimethyl sulfoxide (DMSO). Information about their interactions in solutions and on the stability of the K-peptide was obtained by FTIR spectroscopy and differential scanning microcalorimetry. The IR spectra of various osmolyte–water–model-peptide complexes were simulated with the DFT method (B3LYP/6-311++G(d,p)). The FTIR results indicate that both solutes are neutral for the K-peptide in solution. Both co-solutes affect the peptide to different degrees, as seen in the shape of its amide I band, and have different influences on its thermal stability. DFT calculations helped simplify the experimental data for easier interpretation.

show abstract

“…Various physiochemical conditions have been reported to induce the formation of HEWL fibrils, such as HCl solution of pH 1.6–pH 2.0 at 65°C (Feng et al., 2012; Ow & Dunstan, 2013), glycine solution of pH 2.2 at 57°C (Mahdavimehr et al., 2017). In addition, metal ions such as Cu 2+ in solution of pH 7.0 at 60°C (Bhattacharya et al., 2013) and Al 3+ in solution of pH 2.0 at 60°C (Wawer et al., 2019) can promote HEWL fibrillation. The surfactants like sarkosyl in solution of pH 9.0 (Khan et al., 2018) and sodium dodecyl benzenesulfonate in solution of pH 7.4 (Khan et al., 2019), and food colouring agent like Allura red in solution of pH 7.0 (Al‐Shabib et al., 2019) can also promote the formation of HEWL fibrils.…”

Section: Introductionmentioning

confidence: 99%

Elevated temperatures accelerate the formation of toxic amyloid fibrils of hen egg‐white lysozyme

Feng

Liu

Bai

2021

Veterinary Medicine & Sci

View full text Add to dashboard Cite

The formation of amyloid fibrils is critical for neurodegenerative diseases. Some physiochemical conditions can promote the conversion of proteins from soluble globular shapes into insoluble well‐organized amyloid fibrils. The aim of this study was to investigate the effect of temperatures on amyloid fibrils formation in vitro using the protein model of hen egg‐white lysozyme (HEWL). The HEWL fibrils were prepared at temperatures of 37, 45, 50 and 57°C in glycine solution of pH 2.2. Under transmission electron microscopy, we found the well‐organized HEWL amyloid fibrils at temperatures of 45, 50 and 57°C after 10 days of incubation. Thioflavin T and Congo red florescence assays confirmed that the formation and growth of HEWL fibrils displayed a temperature‐dependent increase, and 57°C produced the most amounts. Meanwhile, the surface hydrophobicity of aggregates was greatly increased by ANS binding assay, and β‐sheet contents by circular dichroism analysis were increased by 17.8%, 22.0% and 34.9%, respectively. Furthermore, the HEWL fibrils formed at 57°C caused significant cytotoxicity in SH‐SY5Y cells after 48 hr exposure, and the cell viability determined by MTT assay was decreased, with 81.35 ± 0.29% for 1 μM, 61.45 ± 2.62% for 2 μM, and 11.58 ± 0.39% (p < .01) for 3 μM. Nuclear staining results also confirmed the apoptosis features. These results suggest that the elevated temperatures could accelerate protein unfolding of the native structure and formation of toxic amyloid fibrils, which can improve understanding the mechanisms of the unfolding and misfolding process of prion protein.

show abstract

Influence of the ionic strength on the amyloid fibrillogenesis of hen egg white lysozyme

Cited by 42 publications

References 38 publications

Influence of Urea and Dimethyl Sulfoxide on K-Peptide Fibrillation

Influence of Urea and Dimethyl Sulfoxide on K-Peptide Fibrillation

DMSO and TMAO—Differences in Interactions in Aqueous Solutions of the K-Peptide

Elevated temperatures accelerate the formation of toxic amyloid fibrils of hen egg‐white lysozyme

Contact Info

Product

Resources

About