Toolkit/Surface plasmon resonance

Surface plasmon resonance

Assay Method·Research·Since 2003

Also known as: SPR

Taxonomy: Technique Branch / Method. Workflows sit above the mechanism and technique branches rather than replacing them.

Summary

Surface plasmon resonance (SPR) ... makes it possible to measure accurately the adsorption of molecules on the metal surface and their eventual interactions with specific ligands.

Usefulness & Problems

Why this is useful

SPR detects refractive index changes near a metal surface to measure molecular adsorption and interactions with specific ligands. The abstract highlights real-time kinetic and label-free biosensing applications.; real-time measurement of ligand-receptor interaction kinetics; lead compound screening; DNA hybridization measurement; enzyme-substrate interaction measurement; polyclonal antibody characterization; epitope mapping; protein conformation studies; label-free immunoassays

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SPR detects refractive index changes near a metal surface to measure molecular adsorption and interactions with specific ligands. The abstract highlights real-time kinetic and label-free biosensing applications.

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real-time measurement of ligand-receptor interaction kinetics

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lead compound screening

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DNA hybridization measurement

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enzyme-substrate interaction measurement

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polyclonal antibody characterization

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epitope mapping

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protein conformation studies

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label-free immunoassays

Problem solved

It enables accurate, label-free, real-time measurement of biomolecular binding and related interaction kinetics across multiple biomedical assay types.; label-free detection of molecular adsorption and binding interactions; real-time monitoring of biomolecular association and dissociation

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It enables accurate, label-free, real-time measurement of biomolecular binding and related interaction kinetics across multiple biomedical assay types.

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label-free detection of molecular adsorption and binding interactions

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real-time monitoring of biomolecular association and dissociation

Problem links

label-free detection of molecular adsorption and binding interactions

Literature

It enables accurate, label-free, real-time measurement of biomolecular binding and related interaction kinetics across multiple biomedical assay types.

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It enables accurate, label-free, real-time measurement of biomolecular binding and related interaction kinetics across multiple biomedical assay types.

real-time monitoring of biomolecular association and dissociation

Literature

It enables accurate, label-free, real-time measurement of biomolecular binding and related interaction kinetics across multiple biomedical assay types.

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It enables accurate, label-free, real-time measurement of biomolecular binding and related interaction kinetics across multiple biomedical assay types.

Taxonomy & Function

Primary hierarchy

Technique Branch

Method: A concrete measurement method used to characterize an engineered system.

Target processes

recombinationselection

Input: Chemical

Implementation Constraints

cofactor dependency: cofactor requirement unknownencoding mode: genetically encodedimplementation constraint: context specific validationoperating role: sensor

The method requires a metal surface, typically gold or silver, and in conventional formats specialized biosensing instruments and immobilized ligands or proteins on sensor chips.; requires metal surfaces such as gold or silver; conventional implementations use specialized biosensing instruments

The abstract notes that conventional SPR can be constrained by expensive chips, limited chip reuse, and complex immobilization chemistry.; conventional SPR uses expensive sensor chips with limited reuse capacity; conventional SPR requires complex chemistry for ligand or protein immobilization

Validation

Cell-freeBacteriaMammalianMouseHumanTherapeuticIndep. Replication

Supporting Sources

Ranked Claims

Claim 1application scopesupports2003Source 1needs review

SPR is applied to real-time measurement of ligand-receptor kinetics, lead compound screening, DNA hybridization, enzyme-substrate interactions, polyclonal antibody characterization, epitope mapping, protein conformation studies, and label-free immunoassays.

The technique is applied not only to the measurement in real‐time of the kinetics of ligand–receptor interactions and to the screening of lead compounds in the pharmaceutical industry, but also to the measurement of DNA hybridization, enzyme–substrate interactions, in polyclonal antibody characterization, epitope mapping, protein conformation studies and label‐free immunoassays.
Claim 2capabilitysupports2003Source 1needs review

Surface plasmon resonance enables accurate measurement of molecular adsorption on metal surfaces and interactions with specific ligands through sensitivity to refractive index changes near the surface.

Biomedical applications take advantage of the exquisite sensitivity of SPR to the refractive index of the medium next to the metal surface, which makes it possible to measure accurately the adsorption of molecules on the metal surface and their eventual interactions with specific ligands.
Claim 3limitationsupports2003Source 1needs review

Conventional SPR relies on specialized biosensing instruments with expensive sensor chips of limited reuse capacity and requires complex chemistry for ligand or protein immobilization.

Conventional SPR is applied in specialized biosensing instruments. These instruments use expensive sensor chips of limited reuse capacity and require complex chemistry for ligand or protein immobilization.

Approval Evidence

1 source3 linked approval claimsfirst-pass slug surface-plasmon-resonance
Surface plasmon resonance (SPR) ... makes it possible to measure accurately the adsorption of molecules on the metal surface and their eventual interactions with specific ligands.

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application scopesupports

SPR is applied to real-time measurement of ligand-receptor kinetics, lead compound screening, DNA hybridization, enzyme-substrate interactions, polyclonal antibody characterization, epitope mapping, protein conformation studies, and label-free immunoassays.

The technique is applied not only to the measurement in real‐time of the kinetics of ligand–receptor interactions and to the screening of lead compounds in the pharmaceutical industry, but also to the measurement of DNA hybridization, enzyme–substrate interactions, in polyclonal antibody characterization, epitope mapping, protein conformation studies and label‐free immunoassays.

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capabilitysupports

Surface plasmon resonance enables accurate measurement of molecular adsorption on metal surfaces and interactions with specific ligands through sensitivity to refractive index changes near the surface.

Biomedical applications take advantage of the exquisite sensitivity of SPR to the refractive index of the medium next to the metal surface, which makes it possible to measure accurately the adsorption of molecules on the metal surface and their eventual interactions with specific ligands.

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limitationsupports

Conventional SPR relies on specialized biosensing instruments with expensive sensor chips of limited reuse capacity and requires complex chemistry for ligand or protein immobilization.

Conventional SPR is applied in specialized biosensing instruments. These instruments use expensive sensor chips of limited reuse capacity and require complex chemistry for ligand or protein immobilization.

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Comparisons

Source-stated alternatives

The paper contrasts conventional instrument-based SPR with the authors' colloidal-gold SPR implementation monitored by UV-vis spectrophotometry.

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The paper contrasts conventional instrument-based SPR with the authors' colloidal-gold SPR implementation monitored by UV-vis spectrophotometry.

Source-backed strengths

exquisite sensitivity to refractive index changes near the metal surface; supports real-time kinetic measurements; label-free measurement modality

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exquisite sensitivity to refractive index changes near the metal surface

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supports real-time kinetic measurements

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label-free measurement modality

Surface plasmon resonance and high-throughput drug screening using hPSC-derived cellular models address a similar problem space because they share recombination, selection.

Shared frame: same top-level item type; shared target processes: recombination, selection; same primary input modality: chemical

Compared with ProKAS

Surface plasmon resonance and ProKAS address a similar problem space because they share recombination, selection.

Shared frame: same top-level item type; shared target processes: recombination, selection; same primary input modality: chemical

Surface plasmon resonance and single-cell RNA sequencing address a similar problem space because they share recombination, selection.

Shared frame: same top-level item type; shared target processes: recombination, selection; same primary input modality: chemical

Relative tradeoffs: appears more independently replicated; looks easier to implement in practice.

Ranked Citations

  1. 1.
    StructuralSource 1Journal of Spectroscopy2003Claim 1Claim 2Claim 3

    Extracted from this source document.