α-Methylation Enables the X-ray Crystallographic Observation of Oligomeric Assemblies Formed by a β-Hairpin Peptide Derived from Aβ DOI Creative Commons
Tuan D. Samdin, Adam G. Kreutzer, Victoria Sahrai

et al.

The Journal of Organic Chemistry, Journal Year: 2024, Volume and Issue: unknown

Published: Dec. 17, 2024

The assembly of the β-amyloid peptide Aβ into toxic oligomers plays a significant role in neurodegeneration associated with pathogenesis Alzheimer's disease. Our laboratory has developed N-methylation as tool to enable X-ray crystallographic studies formed by macrocyclic β-hairpin peptides derived from Aβ. In this investigation, we set out determine whether α-methylation could be used an alternative studying oligomerization α-Methylation permits triangular trimer and ball-shaped dodecamer, resembling assemblies N-methylated homolog. Subtle differences are observed conformation α-methylated when compared Notably, appears promote flatter more extended β-sheet than that β-sheets or typical unmodified β-sheet. provides Aβ, attractive feature preserving NH hydrogen-bond donors along backbone.

Language: Английский

Amyloid–ß peptides interaction with curcumin:AFM and electrochemical characterisation DOI
Ana‐Maria Chiorcea‐Paquim,

Wesley Bruno S. Mascini,

Ana Maria Oliveira‐Brett

et al.

Electrochimica Acta, Journal Year: 2025, Volume and Issue: unknown, P. 146160 - 146160

Published: March 1, 2025

Language: Английский

Citations

0
Structures of Oligomeric States of Tau Protein, Amyloid-β, α-Synuclein and Prion Protein Implicated in Alzheimer’s Disease, Parkinson’s Disease and Prionopathies DOI Open Access
Ondrej Cehlár,

Stefana Njemoga,

Miloš Horváth

et al.

International Journal of Molecular Sciences, Journal Year: 2024, Volume and Issue: 25(23), P. 13049 - 13049

Published: Dec. 4, 2024

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

Language: Английский

Citations

1
Homoplantaginin Antagonizes N-Methyl-d-aspartate Receptor and Extracellular Signal-Regulated Kinase Signaling in Aβ Oligomers-Induced Neuropathology/Toxicity DOI
Ting‐Yu Chen, Yi‐Ru Chen,

Ming-Lung Hsu

et al.

Journal of Agricultural and Food Chemistry, Journal Year: 2024, Volume and Issue: unknown

Published: Dec. 11, 2024

Extracts from plants/herbals are great resources of drugs and nutrients. Baicalein, a component present in

Language: Английский

Citations

1
α-Methylation Enables the X-ray Crystallographic Observation of Oligomeric Assemblies Formed by a β-Hairpin Peptide Derived from Aβ DOI Creative Commons
Tuan D. Samdin, Adam G. Kreutzer, Victoria Sahrai

et al.

The Journal of Organic Chemistry, Journal Year: 2024, Volume and Issue: unknown

Published: Dec. 17, 2024

The assembly of the β-amyloid peptide Aβ into toxic oligomers plays a significant role in neurodegeneration associated with pathogenesis Alzheimer's disease. Our laboratory has developed N-methylation as tool to enable X-ray crystallographic studies formed by macrocyclic β-hairpin peptides derived from Aβ. In this investigation, we set out determine whether α-methylation could be used an alternative studying oligomerization α-Methylation permits triangular trimer and ball-shaped dodecamer, resembling assemblies N-methylated homolog. Subtle differences are observed conformation α-methylated when compared Notably, appears promote flatter more extended β-sheet than that β-sheets or typical unmodified β-sheet. provides Aβ, attractive feature preserving NH hydrogen-bond donors along backbone.

Language: Английский

Citations

1