Real-Time Analysis of Binding Events between Different Aβ1–42 Species and Human Lilrb2 by Dual Polarization Interferometry
Abstract
Abnormal accumulation of 42-residue amyloid-β (Aβ 1–42 ) within the brain triggers the pathogenesis of Alzheimer’s disease (AD). In this paper, we use a dual polarization interferometry (DPI) tool to evaluate the binding events of various Aβ 1–42 species such as monomeric Aβ 1–42, low molecular weight Aβ 1–42 oligomer (LMW Aβ 1–42 ), and high molecular weight Aβ 1–42 oligomer (HMW Aβ 1–42 ) with extracellular D1D2 domain of lilrb2 (ED1D2L) receptor that has been proved to be associated with AD. Based on the real-time binding information provided by DPI, the association rate ( k a ) of ED1D2L receptor with monomeric Aβ 1–42, LMW Aβ 1–42, and HMW Aβ 1–42 is individually determined to be 2.85 × 10 4, 4.52 × 10 4, and 1.34 × 10 5 M –1 ·s –1, and meanwhile, the dissociation rate ( k d ) corresponds to 1.79 × 10 –2, 2.09 × 10 –2, and 5.34 × 10 –4 s –1, respectively. By analysis of the kinetic parameters of k a and k d values, we discovery that the HMW Aβ 1–42 exhibits the fastest rate for ED1D2L receptor in the association phrase, and HMW Aβ 1–42 likewise shows the highest affinity with ED1D2L receptor during the dissociation period in contrast to LMW Aβ 1–42 and monomeric Aβ 1–42 . Our findings significantly reveal the different binding behaviors among them from the perspective of kinetics aspect, by which we could indirectly elucidate the malicious impacts in the process of AD triggered by HMW Aβ 1–42 . Strikingly, this work offers a new exciting clue to explore the dynamic properties associated with interactions of various Aβ 1–42 species with other targets and hopefully contributes to drug discovery and screen in the future.
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SORLA interacts with EphA4 and inhibits Aβ-induced EphA4 activation, thereby reducing oAβ-induced synaptotoxicity.
“In addition, we recently reported that SORLA can interact EphA4 and inhibit Aβ-induced EphA4 activation, thereby reducing oAβ-induced synaptotoxicity [488].”
From Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease (2020) · cites this paper as [488]
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- Authors
- Hu, T., Wang, S., Chen, C., Sun, J., & Yang, X.
- Affiliations
- University of Science and Technology of China (CN)
- Chinese Academy of Sciences (CN)
- Corresponding author
- Sun, Jian
- Yang, Xiurong
- Venue
- Analytical Chemistry
- Publisher
- American Chemical Society (ACS)
- Published
- 2017-02-03
- Volume
- 89
- Issue
- 4
- Pages
- 2606-2612
- ISSN
- 0003-2700 (ISSN-L)
- 1520-6882
- OpenAlex
- W2575102843
- Cited by
- 28
- References
- 46
- Citations by year
- 2026: 3 · 2025: 2 · 2024: 5 · 2023: 5 · 2022: 2 · 2021: 3 · 2020: 3 · 2019: 3 · 2018: 2
- FWCI
- 1.62
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Analytical Chemistry (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Natural Science Foundation of China (21435005, 21627808)
- Chinese Academy of Sciences (QYZDY-SSW-SLH019)
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Keywords
- amyloid-beta 42, LILRB2, Alzheimer's disease, amyloid-beta oligomers, binding kinetics, association rate, dissociation rate, ligand-receptor interactions, dual polarization interferometry
- MeSH terms
- Protein Domains, Humans, Interferometry, Kinetics, Membrane Glycoproteins, Peptide Fragments, Protein Binding, Receptors, Immunologic, Amyloid beta-Peptides, Microscopy, Atomic Force, Immunoprecipitation, HEK293 Cells, Protein Aggregates
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