ArticleScientific reports2023
Anti-nanodisc antibodies specifically capture nanodiscs and facilitate molecular interaction kinetics studies for membrane protein.
Article in Scientific reports, 2023. 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, 10 citations in OpenAlex.
- A Novel Cell-Based High-Throughput Screening Model for Inhibitors Targeting Influenza Virus Hemagglutinin-α-2,6-Sialic Acid Interaction.Biomolecules · 2026Article
- Differential effects of lipid composition on the thermal and functional properties of membrane associated CYP2J2.Protein science : a publication of the Protein Society · 2026Article
- Latest surface plasmon resonance advances for G protein-coupled receptors.Journal of pharmaceutical analysis · 2026Review
- Updates to Guidance on Using Biacore for Protein-Protein Interactions Analysis.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Examining the thermotropic properties of large circularized nanodiscs.Biochimica et biophysica acta. Biomembranes · 2025Article
- Fab-Induced Stabilization of an Ion Channel Receptor Enables Mechanistic Characterization of Small-Molecule Therapeutics.Analytical chemistry · 2025Article
- The Nature of Nanodisc Lipids Influences Fragment-Based Drug Discovery Results.Chemical biology & drug design · 2025Article
Corrections and comments
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Authors and funding
14 authors at 5 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Nanodisc technology has dramatically advanced the analysis of molecular interactions for membrane proteins. A nanodisc is designed as a vehicle for membrane proteins that provide a native-like phospholipid environment and better thermostability in a detergent-free buffer. This enables the determination of the thermodynamic and kinetic parameters of small molecule binding by surface plasmon resonance. In this study, we generated a nanodisc specific anti-MSP (membrane scaffold protein) monoclonal antibody biND5 for molecular interaction analysis of nanodiscs. The antibody, biND5 bound to various types of nanodiscs with sub-nanomolar to nanomolar affinity. Epitope mapping analysis revealed specific recognition of 8 amino acid residues in the exposed helix-4 structure of MSP. Further, we performed kinetics binding analysis between adenosine A
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