ArticleThe journal of physical chemistry letters2021
Combined High-Pressure and Multiquantum NMR and Molecular Simulation Propose a Role for N-Terminal Salt Bridges in Amyloid-Beta.
Article in The journal of physical chemistry letters, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Functionally related internal fluctuations in human ileal bile acid-binding protein by high pressure nuclear magnetic resonance.Protein science : a publication of the Protein Society · 2026Article
- Synthesis and Characterization of a Nanoscale Hyaluronic Acid-Specific Probe for Magnetic Particle Imaging and Magnetic Resonance Imaging.Nanomaterials (Basel, Switzerland) · 2025Article
- Constant pH Molecular Dynamics Simulation of pH Effects on Amyloid-β Structure, Dynamics, and Metal-Binding.Chemistry (Weinheim an der Bergstrasse, Germany) · 2025Article
- Synthesis of SelectivelyChemistry (Weinheim an der Bergstrasse, Germany) · 2025Article
- Autoinhibition in the Signal Transducer CIN85 Modulates B Cell Activation.Journal of the American Chemical Society · 2024Article
- Article
- Sequence-Dependent Backbone Dynamics of Intrinsically Disordered Proteins.Journal of chemical theory and computation · 2022Article
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Authors and funding
4 authors.
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Abstract
Several lines of evidence point to the important role of the N-terminal region of amyloid-beta (Aβ) peptide in its toxic aggregation in Alzheimer's disease (AD). It is known that charge-altering modifications such as Ser8 phosphorylation promote Aβ fibrillar aggregation. In this Letter, we combine high-pressure NMR, multiquantum chemical exchange saturation transfer (MQ-CEST) NMR, and microseconds-long molecular dynamics simulation and provide evidence of the presence of several salt bridges between Arg5 and its nearby negatively charged residues, in particular, Asp7 and Glu3. The presence of these salt bridges is correlated with less extended structures in the N-terminal region of Aβ. Through density functional theory calculations, we demonstrate how the introduction of negatively charged phosphoserine 8 influences the network of adjacent salt bridges in Aβ and favors more extended N-terminal structures. Our data propose a structural mechanism for the Ser8-phosphorylation-promoted Aβ aggregation and define the N-terminal salt bridges as potential targets for anti-AD drug design.
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