Using Sugar-Derived Nanoparticles to Mitigate Amyloid Fibril Formation of Lysozyme

Lai, You-Ren; Wang, Tzu-Horng; How, Su-Chun; Lin, Kuen‐Song; Chou, Wei-Long; Wang, Steven S.‐S.

doi:10.1016/j.jtice.2022.104360

Cited by 6 publications

(3 citation statements)

References 52 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The black line presents the spectra for pure Lys without providing the incubation; here the fluorescence intensity is lowest. The spectra in red color represent the incubated Lys (i.e., the fibrillar form of Lys); the increase in ThT fluorescence intensity confirms the formation of Lys fibrils, which is supported by the liteerature . In the presence of [Chn][Ac], the fluorescence intensity of Lys decreased as compared to that of Lys incubated without IL, while it is still higher than that of the native Lys (Figure a).…”

Section: Resultssupporting

confidence: 52%

“…The antiamyloidogenic action of [Chn] ILs on Lys fibril formation was further appraised by ThT fluorescence spectroscopy analysis; ThT is a sensitive dye used for probing the fibril formation of various proteins . ThT dye, when bound with fibrillar aggregates, exhibits high fluorescence intensity, as it interacts with the grooves of proteins that are exposed to solvents, which are formed through side-chain aromatic amino acids comprising crossed β-strands, and finally gets stabilized. − Figure portrays the ThT fluorescence spectra of native Lys and incubated Lys in the absence and presence of [Chn] ILs. The black line presents the spectra for pure Lys without providing the incubation; here the fluorescence intensity is lowest.…”

Section: Resultsmentioning

confidence: 99%

“…The spectra in red color represent the incubated Lys (i.e., the fibrillar form of Lys); the increase in ThT fluorescence intensity confirms the formation of Lys fibrils, which is supported by the liteerature. 57 In the presence of [Chn][Ac], the fluorescence intensity of Lys decreased as compared to that of Lys incubated without IL, while it is still higher than that of the native Lys (Figure 2a). This observation is attributed to the slight control of fibril formation when the incubation was carried out in the presence of 2 that this effect also depends on the concentration of ILs employed in incubation.…”

Section: ■ Materials and Methodsmentioning

confidence: 98%

See 2 more Smart Citations

Cholinium-Based Ionic Liquids Attenuate the Amyloid Fibril Formation of Lysozyme: A Greener Concept of Antiamyloidogenic Ionic Liquids

Sindhu

Varma

Venkatesu

2022

ACS Sustainable Chem. Eng.

View full text Add to dashboard Cite

Amyloid fibrils share dominant β-sheet structures that form pathological deposits in human organs causing various debilitating neurodegenerative diseases such as type II diabetes, Huntington's, Alzheimer's, and Parkinson's diseases, and thus, the treatment of these amyloid-based diseases is a major overriding concern. Ionic liquids (ILs), being biocompatible solvent medium for proteins, have been introduced as effective antiamyloidogenic agents to prevent the fibrillation process; bio-derived choliniumbased ILs ([Chn] ILs) deserve special attention in view of their inhibitory action on protein amyloid formation to enable the restoration of its biochemical function. Herein, the antiamyloidogenic action of four [Chn] ILs, namely cholinium acetate, and cholinium dihydrogen phosphate [Chn][Dhp], on the in vitro amyloid formation of the lysozyme (Lys) was investigated by applying ThT fluorescence, circular dichroism (CD), and Fourier transform infrared (FT-IR) spectroscopy. Additionally, transmission electronic microscopy (TEM), dynamic light scattering (DLS), and atomic force microscopy (AFM) measurements were also performed to ascertain the morphological changes. Interestingly, with incubation of Lys without ILs there was a substantial increase in thioflavin T (ThT) fluorescence intensity for the Lys, confirming the formation of Lys fibrillar aggregates. The results of FT-IR and UV-CD measurements showed that the Lys secondary structure was retained in the presence of the [Chn][Bit] and [Chn][DHP] ILs, which was lost in the absence of these ILs in the incubating conditions. It was further inferred by morphological analysis via TEM, AFM, and DLS that through thermochemical treatment of Lys, fibrils were formed, and these [Chn] ILs exhibit an increased propensity to suppress the formation of mature fibrils. Overall, the inhibition efficiency of these [Chn] ILs is accredited to the bio-derived cholinium cations as well as the nature of anions based on Hofmeister series. The present study offers a deep insight into the role of ILs in controlling the fibril formation in proteins and thus, they may serve as agents to remediate neurodegenerative diseases.

show abstract

Section: Resultssupporting

confidence: 52%