Fluorescence Resonance Energy Transfer (FRET)-Based ThT Free Sensing of Beta-Amyloid Fibrillation by Carbon Dot-Ag Composites

Nair, Radhika V.; Gulyás, Balázs; Matham, Murukeshan Vadakke

doi:10.1007/s11468-020-01338-w

Cited by 10 publications

(2 citation statements)

References 45 publications

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“…The combination of HEWL with Lys‐CA‐CDs was different from that of BSA. Lys‐CA‐CDs may intercalate into the molecular chain of HEWL and bound to the β‐sheet of HEWL through hydrophobic interactions as well as π‐π packing 50,53 . The secondary structure of HEWL was changed, which made the formation of fibrils become difficult.…”

Section: Discussionmentioning

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: Discussionmentioning

confidence: 99%

“…Lys-CA-CDs may intercalate into the molecular chain of HEWL and bound to the β-sheet of HEWL through hydrophobic interactions as well as π-π packing. 50,53 The secondary struc-…”

Section: Discussionmentioning

confidence: 99%

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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show abstract

Recent Advancements in Biosensors for the Detection and Characterization of Amyloids: A Review

Rashid,

sen

2024

Protein J

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Epigallocatechin gallate-derived carbonized polymer dots: A multifunctional scavenger targeting Alzheimer's β-amyloid plaques

et al. 2023

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Fluorescence Resonance Energy Transfer (FRET)-Based ThT Free Sensing of Beta-Amyloid Fibrillation by Carbon Dot-Ag Composites

Abstract: resonance energy transfer (FRET)-based ThT free sensing of beta-amyloid fibrillation by carbon dot-Ag composites. Plasmonics, 16(3), 863-872.

Cited by 10 publications

References 45 publications

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

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

Recent Advancements in Biosensors for the Detection and Characterization of Amyloids: A Review

Epigallocatechin gallate-derived carbonized polymer dots: A multifunctional scavenger targeting Alzheimer's β-amyloid plaques

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