Effects of amino acid-functionalized silver nanoparticles on lysozyme amyloid fibrillogenesis

Lu, Sophie Shin; Lai, You-Ren; Hsiao, Li-Hsing; Huang, Hsin‐Yi; Tsai, Yu-Chen; Chen, Yun; Wang, Steven S.‐S.; Yeh, Yi Chun; Tsai, Shen‐Long

doi:10.1016/j.colsurfb.2023.113144

Cited by 8 publications

(2 citation statements)

References 53 publications

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“…Nasser Abdulatif Al‐Shabib deciphered the inhibition of rutin on β‐lactoglobulin amyloid aggregation at pH 2.0 and 358 K 11 . Besides these small molecules, polypeptide, polymeric micelles, polymer nanoparticles, and metal nanoparticles also could affect the amyloid aggregation of protein 12–19 . In addition, there were also some reports on amyloid fibrils inducers.…”

Section: Introductionmentioning

confidence: 99%

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Dissimilar effects of the hydrophilic carbon dots on the amyloid aggregation of two model proteins and the mechanism discussion

Li,

Zhang,

Dong

et al. 2024

J of Molecular Recognition

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Many proteins could aggregate into amyloid fibrils under certain conditions. However, the aggregation process and morphology of the fibrils may be significantly different because of the distinct protein structure. In this article, the hydrophilic carbon dots (Lys‐CA‐CDs) were prepared using lysine (Lys) and citric acid (CA) as reactant under the assistance of a microwave. The dissimilar modulation effect of Lys‐CA‐CDs on the aggregation process of distinct structure protein was further investigated, where bovine serum albumin (BSA) and hen egg white lysozyme (HEWL) were chosen as model proteins. All results showed that Lys‐CA‐CDs displayed the contrary influence on the aggregation process of BSA and HEWL. Lys‐CA‐CDs could induce BSA to aggregate into more wormlike fibrils and inhibit the aggregation of HEWL into hair‐like fibrils. The influence on the aggregation process of BSA may be assigned to the increased concentration of BSA around the Lys‐CA‐CDs caused by their interaction. However, inserting of Lys‐CA‐CDs into the inner structure of HEWL led to the change of protein secondary structure. The change of secondary structure further made it difficult for HEWL to aggregate into fibrils and Lys‐CA‐CDs showed the inhibition effect on HEWL aggregation.

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Section: Introductionmentioning

confidence: 99%

“…nanoparticles also could affect the amyloid aggregation of protein. [12][13][14][15][16][17][18][19] In addition, there were also some reports on amyloid fibrils inducers. For example, sodium dodecyl sulphate 20 and sunset yellow dye 21 were reported as inducer on protein amyloid aggregation at appropriate dosage and solution conditions.…”

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confidence: 99%