2022
DOI: 10.1038/s42004-022-00786-1
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Multivariate effects of pH, salt, and Zn2+ ions on Aβ40 fibrillation

Abstract: Amyloid-β (Aβ) peptide aggregation plays a central role in the progress of Alzheimer’s disease (AD), of which Aβ-deposited extracellular amyloid plaques are a major hallmark. The brain micro-environmental variation in AD patients, like local acidification, increased ionic strength, or changed metal ion levels, cooperatively modulates the aggregation of the Aβ peptides. Here, we investigate the multivariate effects of varied pH, ionic strength and Zn2+ on Aβ40 fibrillation kinetics. Our results reveal that Aβ f… Show more

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Cited by 15 publications
(11 citation statements)
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“…Endogenously driven [1,[52][53][54][55][56] Implementation for in vivo and in vitro systems Structurally unstable, stoichiometrically undefined Detergent micelles [24, 26,, 57, 58] Small size ideal for solution NMR and MS measurements Structurally unstable, stoichiometrically undefined Chemical scaffolds [59][60][61][62][63][64] Defined oligomer stoichiometry and structure after chemical modification…”
Section: Methods Advantages Disadvantagesmentioning
confidence: 99%
See 1 more Smart Citation
“…Endogenously driven [1,[52][53][54][55][56] Implementation for in vivo and in vitro systems Structurally unstable, stoichiometrically undefined Detergent micelles [24, 26,, 57, 58] Small size ideal for solution NMR and MS measurements Structurally unstable, stoichiometrically undefined Chemical scaffolds [59][60][61][62][63][64] Defined oligomer stoichiometry and structure after chemical modification…”
Section: Methods Advantages Disadvantagesmentioning
confidence: 99%
“…[54] Aβ oligomer stability and formation rate can be affected by factors such as temperature, ionic strength, and pH. [55,56] For example, higher temperatures and acidic pH can promote the formation of Aβ oligomers, while lower temperatures and neutral pH can inhibit their formation. [56] This sensitivity to solution conditions makes it challenging to characterize the toxic forms of Aβ oligomers, as they can be unstable and heterogeneous.…”
Section: Endogenously Driven Protein Oligomerizationmentioning
confidence: 99%
“…This term can also be temperature-dependent on accounting for the upper and lower critical solution temperatures [ 202 ] and salt-dependent to account for the salting-out effect at high salt concentrations [ 203 ]. Additional angle and dihedral terms can be introduced to capture the residue-specific secondary structure propensities of the chain [ 204 , 205 ]. The entire framework is flexible and easy to re-optimize with growing experimental measurements [ 190 , 199 , 200 , 201 ] and can be extended to biomolecules such as nucleic acids [ 206 ].…”
Section: Theoretical and Computational Biophysical Techniquesmentioning
confidence: 99%
“…Besides, the specific roles of transition metal ions in protein denaturation are well-known as “Hofmeister series” according to the sequence of their action strength. 19 , 20 It is worth noting that the disparate effects of Zn 2+ , 21 , 22 Cu 2+ , 23 , 24 Al 3+ , 25 and Mn 2+ 26 , 27 on denaturation of various proteins were reported. For example, a double-edged effect of Al 3+ ions on the HEWL amyloid fibrillation kinetics has been revealed recently 25 that Al 3+ ions accelerate the conformational transformations from α-helices to organized β-sheets, in addition to postponing α-helix degradation.…”
Section: Introductionmentioning
confidence: 99%
“…Because HEWL in the nature state is resistant to denaturation, previous studies on the denaturation of HEWL were mainly carried out in unnatural conditions, like acidic and thermal treatment. , Moreover, the promotion or inhibition effects of ethanol, guanidine hydrochloride, alkaline pH, sunset yellow, and succinimide, even including silver nanoparticles, were also discussed on amyloid fibrils formation. Besides, the specific roles of transition metal ions in protein denaturation are well-known as “Hofmeister series” according to the sequence of their action strength. , It is worth noting that the disparate effects of Zn 2+ , , Cu 2+ , , Al 3+ , and Mn 2+ , on denaturation of various proteins were reported. For example, a double-edged effect of Al 3+ ions on the HEWL amyloid fibrillation kinetics has been revealed recently that Al 3+ ions accelerate the conformational transformations from α-helices to organized β-sheets, in addition to postponing α-helix degradation.…”
Section: Introductionmentioning
confidence: 99%