SAXS/WAXS Investigation of Amyloid-β(16-22) Peptide Nanotubes

Narayanan, Theyencheri; Rüter, Axel; Olsson, Ulf

doi:10.3389/fbioe.2021.654349

Cited by 9 publications

(6 citation statements)

References 18 publications

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“…The β-strand separation of 4.7 Å is a characteristic feature of parallel and antiparallel β-sheets in folded monomeric proteins as well as in aggregates ( 36 , 37 ) and is observed also in the case of β-sheet aggregates of short peptides ( 38 , 39 ). Interestingly, the characteristic distance of 10 Å is also observed for β-sheet aggregates of the core segment Aβ ( 16 – 22 , 40 ), where it clearly corresponds to the separation between β-sheets in a two-dimensional (2D) crystalline lattice ( 40 ).…”

Section: Resultsmentioning

confidence: 95%

Amyloid β 42 fibril structure based on small-angle scattering

Lattanzi

André

Gasser

et al. 2021

Proc. Natl. Acad. Sci. U.S.A.

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Amyloid fibrils are associated with a number of neurodegenerative diseases, including fibrils of amyloid β42 peptide (Aβ42) in Alzheimer’s disease. These fibrils are a source of toxicity to neuronal cells through surface-catalyzed generation of toxic oligomers. Detailed knowledge of the fibril structure may thus facilitate therapeutic development. We use small-angle scattering to provide information on the fibril cross-section dimension and shape for Aβ42 fibrils prepared in aqueous phosphate buffer at pH = 7.4 and pH 8.0 under quiescent conditions at 37 °C from pure recombinant Aβ42 peptide. Fitting the data using a continuum model reveals an elliptical cross-section and a peptide mass-per-unit length compatible with two filaments of two monomers, four monomers per plane. To provide a more detailed atomistic model, the data were fitted using as a starting state a high-resolution structure of the two-monomer arrangement in filaments from solid-state NMR (Protein Data Bank ID 5kk3). First, a twofold symmetric model including residues 11 to 42 of two monomers in the filament was optimized in terms of twist angle and local packing using Rosetta. A two-filament model was then built and optimized through fitting to the scattering data allowing the two N-termini in each filament to take different conformations, with the same conformation in each of the two filaments. This provides an atomistic model of the fibril with twofold rotation symmetry around the fibril axis. Intriguingly, no polydispersity as regards the number of filaments was observed in our system over separate samples, suggesting that the two-filament arrangement represents a free energy minimum for the Aβ42 fibril.

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Section: Resultsmentioning

confidence: 95%

Amyloid β 42 fibril structure based on small-angle scattering

Lattanzi

André

Gasser

et al. 2021

Proc. Natl. Acad. Sci. U.S.A.

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“…High-concentration solutions increase the number of molecules, thereby reinforcing the capability of self-assembly and aggregating more protein molecules . Recently, the self-assembly of peptide β (16–22) was studied using X-ray scattering over a range of peptide concentrations . The scattering form factor of the nanotubes was significantly enhanced at the concentrations of 0.2 and 0.5% (by weight).…”

Section: Stimulus-responsive Self-assembly Of Fpdmpsmentioning

confidence: 99%

A Comprehensive Review of Self-Assembled Food Protein-Derived Multicomponent Peptides: From Forming Mechanism and Structural Diversity to Applications

Liu

Zhang

et al. 2023

J. Agric. Food Chem.

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Food protein-derived multicomponent peptides (FPDMPs) are a natural blend of numerous peptides with various bioactivities and multiple active sites that can assume several energetically favorable conformations in solutions. The remarkable structural characteristics and functional attributes of FPDMPs make them promising codelivery carriers that can coassemble with different bioactive ingredients to induce multidimensional structures, such as fibrils, nanotubes, and nanospheres, thereby producing specific health benefits. This review offers a prospective analysis of FPDMPs-based self-assembly nanostructures, focusing on the mechanism of formation of self-assembled FPDMPs, the internal and external stimuli affecting peptide self-assembly, and their potential applications. In particular, we introduce the exciting prospect of constructing functional materials through precursor template-induced self-assembly of FPDMPs, which combine the bioactivity and self-assembly capacity of peptides and could dramatically broaden the functional utility of peptide-based materials.

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“…This characteristic peak corresponds to a periodic repeat distance of d β 4.7 Å, and is the repeating β-strand separation in the β-sheets (Serpell et al, 2000). This repeat distance is commonly observed in fibrils formed by other proteins, for example Amyloid-β (Serpell, 2000), as well as for short peptides (Kuczera et al, 2020;Narayanan et al, 2021). The same β-strand repeat distance is also found in fibrils of NACore [αS (68-78)], an 11 residue central segment of αS (Rodriguez et al, 2015;Pallbo et al, 2019).…”

Section: Resultsmentioning

confidence: 83%

Comparing α-Synuclein Fibrils Formed in the Absence and Presence of a Model Lipid Membrane: A Small and Wide-Angle X-Ray Scattering Study

Dubackic¹,

Linse²,

Sparr³

et al. 2022

Front. Soft. Matter

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Amyloid fibrils are associated with a number of different neurodegenerative diseases. Detailed knowledge of the fibril structure will be of importance in the search of therapy and may guide experiments to understand amyloid formation. In this paper we investigate the morphology of α-synuclein amyloid fibrils, associated with Parkinson’s disease, formed under different conditions. In particular, we study, by means of small and wide-angle X-ray scattering, whether the presence of model lipid membranes affect the overall structure of the fibrils formed, motivated by the fact that amyloid fibrils in vivo are formed in a highly lipid-rich environment. Comparing fibrils formed in the presence of lipid with fibrils formed in their absence, show that the presence of lipids has no detectable effect on the fibril cross-section radius and that the characteristic β-strand repeat distance of 4.7 Å of the extended intermolecular β-sheets remains unaffected. We also show that the observed fibril radius is consistent with a fibril structure composed of two protofilaments. This indicates overall that the particular fibril structure, with their stacks of two-dimensionally folded α-synuclein molecules, represent a deep free energy minimum, not largely affected by the co-aggregation with lipids.

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SAXS/WAXS Investigation of Amyloid-β(16-22) Peptide Nanotubes

Cited by 9 publications

References 18 publications

Amyloid β 42 fibril structure based on small-angle scattering

Amyloid β 42 fibril structure based on small-angle scattering

A Comprehensive Review of Self-Assembled Food Protein-Derived Multicomponent Peptides: From Forming Mechanism and Structural Diversity to Applications

Comparing α-Synuclein Fibrils Formed in the Absence and Presence of a Model Lipid Membrane: A Small and Wide-Angle X-Ray Scattering Study

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