ArticleACS sensors2022
Accurate Correction of the "Bulk Response" in Surface Plasmon Resonance Sensing Provides New Insights on Interactions Involving Lysozyme and Poly(ethylene glycol).
Article in ACS sensors, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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Who cites it
6 citing papers in PubMed.
- Multi-parametric interferometric reflectance imaging sensor.Scientific reports · 2026Article
- Review
- Research Progress on Nanomaterials in SPR Sensors.Nanomaterials (Basel, Switzerland) · 2025Review
- Quantitative Detection of Biological Nanoparticles Using Twilight Off-Axis Holographic Microscopy: Insights on Complex Formation between PEGylated Gold Nanoparticles and Lipid Vesicles.The journal of physical chemistry. B · 2025Article
- Tert-Butanol as a Structuring Agent for Cellulose Nanocrystal Fluids and Foams.Biomacromolecules · 2025Article
- Plasmonic biosensors and actuators for integrated point-of-care diagnostics.Npj biosensing · 2025Review
Corrections and comments
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Surface plasmon resonance is a very well-established surface sensitive technique for label-free analysis of biomolecular interactions, generating thousands of publications each year. An inconvenient effect that complicates interpretation of SPR results is the "bulk response" from molecules in solution, which generate signals without really binding to the surface. Here we present a physical model for determining the bulk response contribution and verify its accuracy. Our method does not require a reference channel or a separate surface region. We show that proper subtraction of the bulk response reveals an interaction between poly(ethylene glycol) brushes and the protein lysozyme at physiological conditions. Importantly, we also show that the bulk response correction method implemented in commercial instruments is not generally accurate. Using our method, the equilibrium affinity between polymer and protein is determined to be
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