Surface Plasmon Resonance (SPR) Analysis Service – Real-Time Binding Kinetics with Biacore

Accelerate your research with label-free, real-time biomolecular interaction analysis. Creative Proteomics delivers accurate kinetic, affinity, and mechanism data using advanced Biacore™ platforms—helping you make faster, data-driven decisions in drug discovery, biologics development, and quality assessment.

Ultra-Sensitive Kinetic Profiling – KD range from 10⁻³ to 10⁻¹² M
Minimal Sample Requirement – Only 50–100 μL per assay
Biacore™ T200 & 8K+ Platforms – High-precision and high-throughput analysis
Comprehensive Data Package – Publication-ready figures & expert interpretation
Applicable to Complex Systems – Proteins, peptides, nucleic acids, small molecules

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What Is Surface Plasmon Resonance (SPR) and How Does It Work?

Surface Plasmon Resonance (SPR) is a powerful, label-free analytical technique that enables real-time monitoring of biomolecular interactions. By detecting changes in the refractive index near a sensor surface, SPR provides quantitative kinetic and affinity data without the need for fluorescent or radioactive labeling. This makes it an indispensable tool in drug discovery, protein engineering, and biophysical characterization.

Key Features:

Real-time interaction analysis
Label-free detection
High sensitivity for low-abundance targets
Wide dynamic range for weak to strong binders

Figure 1. Pictorial representation of the SPR principle - Creative Proteomics

Typical Scientific Questions Surface Plasmon Resonance Can Answer

What is the binding affinity (KD) between a ligand and its target?
How fast do molecules associate and dissociate (ka, kd)?
Does my candidate bind specifically to the intended target?
How does a mutation or modification affect binding kinetics?
Can multiple candidates be ranked based on binding strength?
Does my compound act as an inhibitor or competitor?
What is the stoichiometry of the interaction (1:1 or complex)?

Advantages of Our Surface Plasmon Resonance Service

Minimal Sample Requirement — Preserve Valuable Materials

Perform comprehensive kinetic and affinity studies with only small microliter volumes of sample, ideal for scarce or costly biomolecules.

Label-Free Technology — Maintain Native State Integrity

Analyze biomolecular interactions without fluorescent or radioactive labeling, ensuring results reflect authentic, unmodified behavior.

Real-Time Monitoring — Immediate Data Acquisition

Track association and dissociation events as they occur, providing dynamic insight into binding mechanisms and interaction stability.

Broad Dynamic Range — Accurate Measurement Across Affinities

Quantify equilibrium dissociation constants (KD) from millimolar to picomolar levels, accommodating both weak and strong binding interactions.

High Sensitivity Detection — Capture Low-Abundance Events

Detect minute changes in surface mass density with a sensitivity threshold of <1 pg/mm², enabling reliable measurements for challenging analytes.

High-Throughput Capability — Accelerate Candidate Screening

Leverage multi-channel SPR systems to process numerous interaction pairs in a single run, reducing time and improving efficiency for large-scale projects.

Technical Services

Service Scope Workflow and Instrumentation Application Sample Requirement Deliverables FAQ Get a Custom Proposal

Scope of Surface Plasmon Resonance Services at Creative Proteomics

Kinetic & Affinity Analysis

Determine association/dissociation rates (ka, kd) and KD values for any biomolecular pair.

Epitope Mapping & Binning

Characterize antibody binding sites to support therapeutic development.

Competition & Inhibition Assays

Evaluate multi-ligand binding and mechanism-of-action profiles.

Fragment-Based Screening

Identify low-affinity hits for early-stage drug discovery.

Small Molecule Interaction Analysis

Rapidly assess binding of compound libraries to target proteins.

Concentration Analysis

Quantify active analytes in complex matrices with high specificity.

Batch Comparability & Quality Assessment

Ensure consistency in biologics or biosimilar production.

Custom Sensor Chip Development

Design tailored immobilization strategies for difficult targets like membrane proteins.

Analyte Types Supported:

Protein–protein interactions (e.g., enzyme–inhibitor, receptor–ligand)
Antibody–antigen binding (including epitope mapping)
Protein–peptide complexes
Protein–small molecule binding
Protein–nucleic acid interactions (DNA/RNA, aptamers)
Protein–carbohydrate interactions
Lipid–protein or membrane-associated complexes
Multi-component assemblies such as receptor–ligand systems, signaling complexes

Our Surface Plasmon Resonance Service Workflow

Workflow for Isothermal Titration Calorimetry

Project Consultation & Assay Design

Define study objectives and choose optimal sensor chip chemistry (e.g., CM5, NTA) and immobilization strategy. Tailor buffer, pH, and regeneration conditions for robust data.

Sample Preparation & Quality Check

Verify sample purity (≥95%), confirm buffer compatibility, and ensure required concentrations (proteins: 0.1–10 mg/mL; small molecules: ≥10 µM). Pre-filtration is recommended for complex samples.

Sensor Chip Functionalization

Immobilize ligands via amine, thiol, His-tag capture, or custom methods. Optimize immobilization level to avoid mass transport limitations.

Real-Time SPR Analysis

Measure association and dissociation phases at multiple analyte concentrations under controlled flow. Include replicate injections for reproducibility.

Data Processing & Modeling

Apply double-referencing and global/local fitting (e.g., 1:1 Langmuir, bivalent models). Perform residual checks and χ² validation for accuracy.

Comprehensive Report Delivery

Receive raw sensorgrams, kinetic constants (ka, kd, KD), fitted curves, and optional thermodynamic data in a publication-ready report with expert interpretation.

Surface Plasmon Resonance Instrumentation & Technical Capabilities

Biacore™ T200 – Ideal for precise kinetic and affinity measurements across diverse interaction types.

Biacore™ 8K+ – High-throughput SPR system optimized for large-scale screening and complex assay formats.

Technical Specifications

Detection Limit: < 1 pg/mm² surface mass change for ultra-sensitive detection
Affinity Range: KD from 10⁻³ to 10⁻¹² M, accommodating weak to strong binders
Sample Volume: Requires as little as 50–100 µL, preserving valuable material
High Throughput: Biacore 8K+ supports up to 768 interactions in a single run
Regeneration Capability: Multiple reuse cycles of sensor chips for cost efficiency
Temperature Control: 4°C to 45°C for stability and thermodynamic studies

Advanced Analytical Features

Kinetic & Affinity Profiling – Real-time association/dissociation monitoring
Thermodynamic Analysis – Evaluate enthalpic and entropic contributions
Custom Sensor Chip Chemistry – Amine coupling, thiol coupling, capture-based strategies

Biacore T200

Biacore 8K+

Application Scenarios

Drug Discovery and Hit-to-Lead Optimization

Identify and rank promising compounds based on binding strength and kinetics, accelerating lead optimization for small-molecule drugs.

Biologics and Antibody Development

Validate antibody-antigen binding, assess epitope diversity, and select high-affinity candidates for therapeutic programs.

Vaccine and Immunotherapy Design

Support epitope binning, antigen mapping, and immune-target validation to improve vaccine formulations and immunotherapeutic strategies.

Protein Engineering and Mutagenesis Studies

Analyze the impact of structural modifications or amino acid substitutions on interaction kinetics and stability.

Biomarker Discovery and Diagnostic Validation

Confirm binding specificity and characterize interaction strength for emerging diagnostic biomarkers.

Regulatory and Quality Comparability Studies

Ensure batch-to-batch consistency in biologics or biosimilars to meet regulatory standards and guarantee therapeutic efficacy.

Mechanism-of-Action Characterization

Evaluate competitive binding or inhibitor potency to elucidate molecular interaction mechanisms in drug and antibody programs.

Early-Stage Fragment-Based Drug Discovery

Enable rapid detection of low-affinity fragments to support fragment growing and linking strategies during early-phase screening.

Sample Requirements for Surface Plasmon Resonance Projects

Parameter	Requirement / Guideline
Sample Type	Proteins, peptides, nucleic acids, small molecules
Purity	≥95% for proteins; small molecules must be analytically pure
Concentration	Proteins: 0.1–10 mg/mL; small molecules: ≥10 μM
Volume	Minimum 50–100 μL per sample
Buffer Conditions	SPR-compatible buffer (e.g., PBS, HEPES); avoid detergents
Additives	Avoid glycerol, Tween, high-salt solutions unless validated
Stability	Store at 4°C or per material requirement; no freeze-thaw cycles
Special Notes	Small molecules should be soluble in assay buffer or DMSO ≤1%

Deliverables: What You Get from Our SPR Service

Raw Sensorgrams – Real-time binding curves showing association and dissociation phases.
Processed Kinetic and Affinity Data – Includes ka, kd, and KD values with confidence intervals.
Thermodynamic Parameters (if requested) – Enthalpy, entropy contributions for deeper interaction insights.
Global and Local Fitting Models – Graphical representations with goodness-of-fit metrics.
Comprehensive Interpretation Report – Summarizing methods, key findings, and recommendations for next steps.

Sensorgram displaying association and dissociation curves for biomolecular interactions measured by SPR at different analyte concentrations.

Sensorgram showing real-time binding responses at multiple analyte concentrations.

Association and dissociation phases are clearly observed, illustrating the kinetics of ligand-analyte interactions under SPR analysis.

Kinetic fitting plot showing experimental SPR sensorgram data and fitted curve for interaction analysis.

Kinetic fitting of experimental SPR data to a 1:1 binding model.

Experimental data points (purple dots) and fitted curve (dashed line) demonstrate excellent agreement, confirming reliable kinetic parameters.

Kinetic fitting of experimental SPR data to a 1:1 binding model.

Experimental data points (purple dots) and fitted curve (dashed line) demonstrate excellent agreement, confirming reliable kinetic parameters.

SPR competition assay curve showing inhibitor concentration versus response for binding inhibition analysis.

Competition binding assay performed by SPR.

Dose-dependent inhibition curve demonstrates the effect of inhibitor concentration on binding response, enabling IC50 determination.

Surface Plasmon Resonance vs Other Structural Analysis Techniques: Which Should You Choose?

Feature	Surface Plasmon Resonance (CD)	FTIR	Fluorescence	NMR	X-ray Crystallography	DSC
Structural Insight	Secondary & Tertiary Structure	Secondary Structure	Tertiary Structure (local)	Atomic-level 3D Structure	Atomic-level 3D Structure	No Structure (Thermal Only)
Sample State	Solution	Solution	Solution	Solution	Crystal	Solution
Sample Amount	50–100 μg	~100 μg	<50 μg	>5 mg	mg-level	>0.5 mg
Analysis Speed	Minutes	Minutes	Minutes	Days–Weeks	Weeks	Hours
Quantitative Accuracy	±5% for Secondary Structure	Moderate	Low	High	High	N/A
Thermal Stability Testing	Yes (with structural correlation)	Limited	Yes (qualitative)	No	No	Yes (detailed thermogram)
Cost Level	Moderate	Low	Low	High	High	Moderate
Data Interpretation	Easy	Moderate	Easy	Complex	Complex	Moderate
Best Use Case	Folding & Stability Screening	Buffer-Insensitive Conditions	Detecting Local Tertiary Changes	High-Resolution Structural Study	Binding Site Mapping for Drug Design	Thermal Stability Only

You May Want to Know

Can SPR measure interactions involving very small molecules or fragments?

Yes. SPR is highly sensitive and can accurately measure interactions with small molecules and fragments, provided they induce sufficient refractive index changes on the sensor surface. Our Biacore™ platforms are optimized for fragment-based screening and small-molecule binding analysis.

What type of binding models can be analyzed with SPR data?

SPR supports multiple kinetic models, including 1:1 Langmuir binding, heterogeneous ligand binding, bivalent analyte interactions, and competition models. Our experts select the appropriate model based on your system's complexity to ensure reliable interpretation.

Can SPR detect weak or transient interactions?

Yes. With an affinity detection range from millimolar to picomolar (KD) and high-resolution instrumentation, SPR can capture weak or transient interactions, provided samples meet purity and concentration requirements.

How does SPR compare with other interaction analysis methods like ITC or ELISA?

SPR provides real-time kinetic data without labeling, which ITC and ELISA cannot deliver. ITC offers thermodynamic information but requires large sample amounts, while ELISA provides endpoint measurements only. SPR combines speed, low sample consumption, and kinetic insight.

Can SPR be used for epitope mapping and binning of antibodies?

Yes. SPR is widely used for epitope characterization and binning studies, allowing comparison of multiple antibodies' binding profiles against the same antigen. This helps in antibody selection and development of therapeutic candidates.

Is thermodynamic analysis possible with SPR?

Yes. By performing experiments at multiple temperatures, SPR can provide insights into enthalpic and entropic contributions to binding, which is valuable for understanding interaction mechanisms and stability.

How does chip regeneration work in SPR?

Chip regeneration involves removing the bound analyte without damaging the immobilized ligand. This allows multiple interaction cycles on the same chip, improving efficiency and reducing costs. Our team selects regeneration conditions specific to your biomolecules.