ArticleBiophysical journal2011
Stoichiometry and affinity of the human serum albumin-Alzheimer's Aβ peptide interactions.
Article in Biophysical journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 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
33 citing papers in PubMed, 90 citations in OpenAlex.
- Binding of Pro-Inflammatory Proteins S100A8 or S100A9 to Amyloid-β Peptide Suppresses Its Fibrillation.Biomolecules · 2025Article
- Inhibition of toxic metal-alpha synuclein interactions by human serum albumin.Chemical science · 2024Article
- Detection of plasma Aβ seeding activity by a newly developed analyzer for diagnosis of Alzheimer's disease.Alzheimer's research & therapy · 2022Article
- Extracellular protein components of amyloid plaques and their roles in Alzheimer's disease pathology.Molecular neurodegeneration · 2021Review
- Antimicrobial and Amyloidogenic Activity of Peptides. Can Antimicrobial Peptides Be Used against SARS-CoV-2?International journal of molecular sciences · 2020Review
- Human Serum Albumin Binds Native Insulin and Aggregable Insulin Fragments and Inhibits Their Aggregation.Biomolecules · 2020Article
- Catechins as Tools to Understand the Molecular Basis of Neurodegeneration.Molecules (Basel, Switzerland) · 2020Review
- Albumin Alters the Conformational Ensemble of Amyloid-β by Promiscuous Interactions: Implications for Amyloid Inhibition.Frontiers in molecular biosciences · 2020Article
- 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
- Therapeutic potency of substituted chromones as Alzheimer's drug: Elucidation of acetylcholinesterase inhibitory activity through spectroscopic and molecular modelling investigation.BioImpacts : BI · 2019Article
- Albumin Exchange in Alzheimer's Disease: Might CSF Be an Alternative Route to Plasma?Frontiers in neurology · 2019Article
- 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
- Chemically treated plasma Aβ is a potential blood-based biomarker for screening cerebral amyloid deposition.Alzheimer's research & therapy · 2017Article
- In Vitro Mouse and Human Serum Stability of a Heterobivalent Dual-Target Probe That Has Strong Affinity to Gastrin-Releasing Peptide and Neuropeptide Y1 Receptors on Tumor Cells.Cancer biotherapy & radiopharmaceuticals · 2017Article
- Fluorescent filter-trap assay for amyloid fibril formation kinetics in complex solutions.ACS chemical neuroscience · 2015Article
- Insulin-degrading enzyme prevents α-synuclein fibril formation in a nonproteolytical manner.Scientific reports · 2015Article
- Amyloid β Protein and Alzheimer's Disease: When Computer Simulations Complement Experimental Studies.Chemical reviews · 2015Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A promising strategy to control the aggregation of the Alzheimer's Aβ peptide in the brain is the clearance of Aβ from the central nervous system into the peripheral blood plasma. Among plasma proteins, human serum albumin plays a critical role in the Aβ clearance to the peripheral sink by binding to Aβ oligomers and preventing further growth into fibrils. However, the stoichiometry and the affinities of the albumin-Aβ oligomer interactions are still to be fully characterized. For this purpose, here we investigate the Aβ oligomer-albumin complexes through a novel and generally applicable experimental strategy combining saturation transfer and off-resonance relaxation NMR experiments with ultrafiltration, domain deletions, and dynamic light scattering. Our results show that the Aβ oligomers are recognized by albumin through sites that are evenly partitioned across the three albumin domains and that bind the Aβ oligomers with similar dissociation constants in the 1-100 nM range, as assessed based on a Scatchard-like model of the albumin inhibition isotherms. Our data not only explain why albumin is able to inhibit amyloid formation at physiological nM Aβ concentrations, but are also consistent with the presence of a single high affinity albumin-binding site per Aβ protofibril, which avoids the formation of extended insoluble aggregates.
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Registered trials
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.