Thermodynamics of oligomerization and Helix-to-sheet structural transition of amyloid β-protein on anionic phospholipid vesicles

Ikeda, Keisuke; Sugiura, Yuuki; Nakao, Hiroyuki; Nakano, Minoru

doi:10.1016/j.bpc.2024.107248

Biophysical Chemistry

2024

DOI: 10.1016/j.bpc.2024.107248

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Thermodynamics of oligomerization and Helix-to-sheet structural transition of amyloid β-protein on anionic phospholipid vesicles

Keisuke Ikeda,

Yuuki Sugiura,

Hiroyuki Nakao

et al.

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2024

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Cited by 3 publications

References 53 publications

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Accelerated Amyloid Aggregation Dynamics of Intrinsically Disordered Proteins in Heavy Water

Son,

Im,

Hyun

et al. 2024

J. Phys. Chem. Lett.

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We explored the influence of D 2 O on the fibrillation kinetics and structural dynamics of amyloid intrinsically disordered proteins (IDPs), including α-synuclein, amyloid-β 1−42, and K18. Our findings revealed that fibrillation of IDPs was accelerated in D 2 O compared to that in H 2 O, exhibiting faster kinetics in contrast to the structured protein, insulin. Structural investigations using electrospray ionization ion mobility mass spectrometry and small-angle Xray scattering combined with molecular dynamics simulations demonstrated that IDPs did not show significant structural changes that could influence accelerated fibrillation in D 2 O. Umbrella sampling of protein protofibrils verified that an increased level of hydrogen bonding of D 2 O and enhanced hydrophobic interactions stabilized β-sheet structured fibrils in D 2 O. These findings indicate that stabilizing β-sheet fibrils and a more hydrophobic microenvironment in D 2 O result in enhanced and faster fibrillation of IDPs. The study highlights the importance of considering D 2 O's differential impact on protein interactions when conducting structural and kinetic analyses, particularly for native peptides and proteins.

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Accelerated Amyloid Aggregation Dynamics of Intrinsically Disordered Proteins in Heavy Water

Son,

Im,

Hyun

et al. 2024

J. Phys. Chem. Lett.

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Mouse brain contains age-dependent extraparenchymal granular structures and astrocytes, both reactive to natural IgM antibodies, linked to the fissura magna

Romera,

Riba,

Alsina

et al. 2024

Immun Ageing

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Structures of Oligomeric States of Tau Protein, Amyloid-β, α-Synuclein and Prion Protein Implicated in Alzheimer’s Disease, Parkinson’s Disease and Prionopathies

Cehlar,

Njemoga,

Horvath

et al. 2024

IJMS

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In this review, we focus on the biophysical and structural aspects of the oligomeric states of physiologically intrinsically disordered proteins and peptides tau, amyloid-β and α-synuclein and partly disordered prion protein and their isolations from animal models and human brains. These protein states may be the most toxic agents in the pathogenesis of Alzheimer’s and Parkinson’s disease. It was shown that oligomers are important players in the aggregation cascade of these proteins. The structural information about these structural states has been provided by methods such as solution and solid-state NMR, cryo-EM, crosslinking mass spectrometry, AFM, TEM, etc., as well as from hybrid structural biology approaches combining experiments with computational modelling and simulations. The reliable structural models of these protein states may provide valuable information for future drug design and therapies.

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Thermodynamics of oligomerization and Helix-to-sheet structural transition of amyloid β-protein on anionic phospholipid vesicles

Cited by 3 publications

References 53 publications

Accelerated Amyloid Aggregation Dynamics of Intrinsically Disordered Proteins in Heavy Water

Accelerated Amyloid Aggregation Dynamics of Intrinsically Disordered Proteins in Heavy Water

Mouse brain contains age-dependent extraparenchymal granular structures and astrocytes, both reactive to natural IgM antibodies, linked to the fissura magna

Structures of Oligomeric States of Tau Protein, Amyloid-β, α-Synuclein and Prion Protein Implicated in Alzheimer’s Disease, Parkinson’s Disease and Prionopathies

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