SPR-Simulation

SPR simulation logoThe SPR-Simulation program is a standalone application to simulate kinetic interaction curves. The program draws the curves after the input of the kinetic rate constants, the analyte concentration and the association and dissociation times. Other features are the simulation of equilibrium sensorgrams and plotting an overlay over an imported sensorgram figure.

SPR-Simulation is capable of the following simulations:

  • Multi cycle kintics
  • Single cycle kinetics
  • Equilibrium kinetics
  • 1:1 kinetics on a decaying surface
  • 1:1 kinetics with mass transfer

The program can export the sensorgrams in Bitmap, SVG and PNG-format. In addition, the curves can be exported in CSV-format compatible with Excel. The result tables can also be copied.

The simulation of interaction curves based on the fitting results can give extra information to improve the experimental set-up.

You can download the manual of the SPR-Simulation program to see if this program can help you with your experiments.

 
Kinetic simulation
Kinetic simulation

Buy SPR-Simulation

The SPR-Simulation program is available for a small fee. With this fee the SPR-pages are maintained and SPR-Simulation program is further developed.

Click the PayPal button to pay and download:


€ 9.95

Screen shots

Single cycle kinetics
Single cycle kinetics

Equilibrium simulation
Equilibrium simulation
Mass transfer
1:1 with mass transfer simulation

LSPR

LSPR instruments utilize a broad band white light source such as an LED to illuminate the nanoparticle sensor substrate. A spectrometer serves as the detector and can be placed in either a transmission or reflection arrangement. The spectrometer provides a reading of the absorbance spectrum of the sensor substrate. The nanoparticle substrates have a characteristic absorbance peak in the visible spectrum due to the LSPR effect. The properties of this absorbance peak (spectral position, absorbance height) are dependent on the local optical properties surrounding the nanoparticles. When a molecule binds to the surface of the nanoparticle, it changes the local optical properties and causes the absorbance peak to change. The properties of the absorbance peak can be monitoring in real-time, providing time resolved molecular analysis on the nanoscale. The size, shape, and material of the nanoparticles can be tuned in order to maximize sensor performance for specific applications.

LSPR principle
LSPR principle

Download more information from Nicoya Lifesciences.


Nicoya LifesciencesOpenSPR by Nicoya Lifesciences utilizes localized surface plasmon resonance (LSPR) for label-free analysis. LSPR is similar to SPR, but it uses nanoparticles of gold rather than a continuous gold film to produce an optical resonance. LSPR’s main advantages are simplicity of the optical design, highly tunable optical properties, no need for temperature control, and robustness. Nicoya has developed a proprietary manufacturing process to create nanoparticle sensors that are highly uniform and stable. Sensors can be functionalized using standard immobilization and coupling chemistry.

Visit Nicoya Lifesciences
Nicoya OpenSPR-XT
OpenSPR-XT

Nanotemper

Light scattering

WhyattWyatt Technology Corp., based in Santa Barbara, CA, is the leading provider of analytical light scattering instrumentation for macromolecular characterization. While Wyatt detectors are most often used in combination with chromatography for determining absolute molar mass and size of macromolecules and particles in solution, the Calypso™ system is a novel application of light scattering, characterizing macromolecular interactions by means of Composition-Gradient Multi-Angle static Light Scattering (CG-MALS). CG-MALS measurements require no labeling or immobilization, for true free-solution, unmodified equilibrium and kinetic measurements to determine stoichiometry, binding affinity and kinetic rates. CG-MALS also characterizes non-specific interactions general solution-dependent attraction or repulsion between molecules that affect stability, aggregation, crystallization and purification.

Bio-Layer Interferometry

ForteBioThe Octet system from Forté Bio™ is using Bio-Layer Interferometry (BLI) to detect binding of biomolecules in real time. Because BLI only detects binding to the senor surface, there is minimal interference from biological sample media. Proteins can be assayed in cell culture media or crude lysates without interference. The machine can read 8 sensors simultanously which can be pre coated or modified by the customer.

Bio-Layer Interferometry (BLI)
FBbli needleThe Octet System utilizes proprietary single-use biosensors with an optical coating layer at the tip of each sensor. This optical surface is coated with a biocompatible matrix that can interact with molecules from a surrounding solution. The Octet instrument shines white light down the biosensor and collects the light reflected back. Reflected light originates from the interface with the optical layer (a) and from the surface of the biocompatible layer (b) where it meets the surrounding solution. FBbli 4 When light waves propagate back from the two reflecting surfaces they interact; some wavelengths show constructive interference, others destructive interference. This interference is captured by a spectrometer as a pattern of intensity variation by wavelength with a characteristic profile of peaks and troughs.

FB Octet
FortéBio Octet