ArticleBiophysical journal2013
Mapping the interactions between the Alzheimer's Aβ-peptide and human serum albumin beyond domain resolution.
Article in Biophysical journal, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
22 citing papers in PubMed, 76 citations in OpenAlex.
- Modulation of islet amyloid polypeptide induced β-cell toxicity and amyloid formation by serum albumin proteins.Biophysical chemistry · 2026Article
- A quantitative Lewy-fold-specific alpha-synuclein seed amplification assay as a progression marker for Parkinson's disease.Acta neuropathologica · 2025Article
- In Search for Low-Molecular-Weight Ligands of Human Serum Albumin That Affect Its Affinity for Monomeric Amyloid β Peptide.International journal of molecular sciences · 2024Article
- Inhibition of toxic metal-alpha synuclein interactions by human serum albumin.Chemical science · 2024Article
- Noncanonical protein kinase A activation by oligomerization of regulatory subunits as revealed by inherited Carney complex mutations.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- A CEST NMR experiment to obtain glycineJournal of biomolecular NMR · 2020Article
- Catechins as Tools to Understand the Molecular Basis of Neurodegeneration.Molecules (Basel, Switzerland) · 2020Review
- Potential sources of interference with the highly sensitive detection and quantification of alpha-synuclein seeds by qRT-QuIC.FEBS open bio · 2020Article
- Albumin Alters the Conformational Ensemble of Amyloid-β by Promiscuous Interactions: Implications for Amyloid Inhibition.Frontiers in molecular biosciences · 2020Article
- Differential Roles of Plasma Protein Corona on Immune Cell Association and Cytokine Secretion of Oligomeric and Fibrillar Beta-Amyloid.Biomacromolecules · 2019Article
- Mechanisms of Specific versus Nonspecific Interactions of Aggregation-Prone Inhibitors and Attenuators.Journal of medicinal chemistry · 2019Article
- Fatty Acids Compete with Aβ in Binding to Serum Albumin by Quenching Its Conformational Flexibility.Biophysical journal · 2019Article
- Human Albumin Impairs Amyloid β-peptide Fibrillation Through its C-terminus: From docking Modeling to Protection Against Neurotoxicity in Alzheimer's disease.Computational and structural biotechnology journal · 2019Article
- C-terminal calcium binding of α-synuclein modulates synaptic vesicle interaction.Nature communications · 2018Article
- Mechanisms of recognition of amyloid-β (Aβ) monomer, oligomer, and fibril by homologous antibodies.The Journal of biological chemistry · 2017Article
- Atomic-resolution map of the interactions between an amyloid inhibitor protein and amyloid β (Aβ) peptides in the monomer and protofibril states.The Journal of biological chemistry · 2017Article
- Albumin nanostructures as advanced drug delivery systems.Expert opinion on drug delivery · 2016Review
- Neuronal uptake of serum albumin is associated with neuron damage during the development of epilepsy.Experimental and therapeutic medicine · 2016Article
- Synergistic Inhibition of Protein Fibrillation by Proline and Sorbitol: Biophysical Investigations.PloS one · 2016Article
- Insulin-degrading enzyme prevents α-synuclein fibril formation in a nonproteolytical manner.Scientific reports · 2015Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Human serum albumin (HSA) is a potent inhibitor of Aβ self-association and this novel, to our knowledge, function of HSA is of potential therapeutic interest for the treatment of Alzheimer's disease. It is known that HSA interacts with Aβ oligomers through binding sites evenly partitioned across the three albumin domains and with comparable affinities. However, as of this writing, no information is available on the HSA-Aβ interactions beyond domain resolution. Here, we map the HSA-Aβ interactions at subdomain and peptide resolution. We show that each separate subdomain of HSA domain 3 inhibits Aβ self-association. We also show that fatty acids (FAs) compete with Aβ oligomers for binding to domain 3, but the determinant of the HSA/Aβ oligomer interactions are markedly distinct from those of FAs. Although salt bridges with the FA carboxylate determine the FA binding affinities, hydrophobic contacts are pivotal for Aβ oligomer recognition. Specifically, we identified a site of Aβ oligomer recognition that spans the HSA (494-515) region and aligns with the central hydrophobic core of Aβ. The HSA (495-515) segment includes residues affected by FA binding and this segment is prone to self-associate into β-amyloids, suggesting that sites involved in fibrilization may provide a lead to develop inhibitors of Aβ self-association.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.