Application Notes

These application notes give examples of some common surface plasmon resonance and label-free analysis applications.

Temperature Dependent Binding Kinetics of Protein-Protein Interactions Using OpenSPR™

Studying protein-protein interactions are important for understanding biological processes at both cellular and systems levels. Surface Plasmon Resonance is a technique used for analyzing the kinetics and affinity of biomolecular interactions, which can also be used to determine thermodynamic parameters. In our new application note, we demonstrate how OpenSPR’s Temperature Control Add-On can be used to analyze the effect of temperature on the kinetics and affinity of a protein-protein interaction.

Binding Kinetics of Therapeutic Monoclonal Antibodies to the CD16a Fc Receptor using OpenSPR™

CD16a (FcуRIIIA) is an Fc receptor protein found on the surface of certain immune cells. CD16a binds to the Fc region of immunoglobulin G (IgG). CD16a-IgG binding initiates antibody-dependent cellular cytotoxicity (ADCC), an important effector mechanism of the immune system. CD16a assays are essential for the development and production of therapeutic monoclonal antibody (mAbs). In this application note, OpenSPR™ is used to successfully determine the binding kinetics and affinity of human CD16a interacting with human IgG (Fc region).

Binding Kinetics of Aptamer-Protein Interactions using OpenSPR™

Aptamers are similar to antibodies in their ability to recognize specific targets, but have a number of potential advantages. However, being a new technology, it is important that characterize tools are developed that can accurately analyze the binding capabilities of aptamers. Surface plasmon resonance is one of the most important tools in characterizing aptamer binding capabilities as it can determine the kinetics and affinity of the interaction in real-time and without the need for labeling. In this application note, we demonstrate how OpenSPR can be used to analyze the binding kinetics of an aptamer-protein interaction.

Binding Kinetics of Glycoprotein Interactions using OpenSPR™

Surface plasmon resonance (SPR) is a commonly used technique for analyzing the binding kinetics of carbohydrate interactions, such as those between glycans, lectins, glycoproteins, glycolipids, proteins and more. In this application note we provide an example of how these types of interactions can be examined using OpenSPR.

Binding Kinetics of Protein-Lipid Interactions using OpenSPR™

Surface plasmon resonance (SPR) is a commonly used technique for analyzing the binding kinetics of protein interactions. One interaction that is especially interesting to examine is the interaction between proteins and lipids. In this application note we provide an example of how these types of interactions can be examined using OpenSPR.

Binding Kinetics of Protein-Protein Interactions using OpenSPR™

One of the most common applications of surface plasmon resonance is the analysis and quantification of the interactions between proteins. In this application note, OpenSPR™ is used to analyze the kon, koff, and KD of two different protein ligands (M1 and M2) to one protein analyte.

Comparison Study of Binding Kinetics on OpenSPR, Biacore and IBIS

OpenSPR™ is a powerful instrument providing indepth label-free binding kinetics for a variety of different molecular interactions. With any new technology, it is important to compare the performance of various tools and techniques to establish their consistency and accuracy.

Kinetic Analysis of High Affinity Antibody Antigen Interaction using Surface Plasmon Resonance

OpenSPR allows users to easily and accurately measure the binding kinetics of numerous ligand-antigen systems. OpenSPR is used to determine the on and off rates and affinity constant for the interaction between prostate specific antigen (PSA) and its antibody (anti-PSA). Results are compared against industry standard surface plasmon resonance instruments.

Binding Kinetics of Calmodulin with Target Peptide of Nitric Oxide Synthase using Surface Plasmon Resonance

OpenSPR can be used to determine the kinetic binding constants of protein-peptide interactions. In this application note, the on and off rates and affinity constant for the interaction between wild type CaM and NOS peptide are determined. Results are compared against the affinity constant obtained from a binding competition assay in the literature.

Biotin-Streptavidin Interaction with OpenSPR System

The interaction between biotin and streptavidin is one of the strongest and most robust interactions that can be studied using SPR. Using the Biotin Streptavidin Training Kit, users can experiment on the OpenSPR system and become more familiar with its capabilities without using up precious material. In this Application Note, we outline the basic protocol to perform biotin-streptavidin tests and give examples of typical results that can be expected.

Surface Plasmon Resonance Refractive Index Sensing using OpenSPEC

OpenSPEC is a powerful visible absorbance spectrophotometer that can be used for a host of applications, such as colorimetric assays, enzyme kinetics, chemical quantification, and more. The SPR capabilities of OpenSPEC are demonstrated by quantifying changes in the bulk refractive index of a solution upon addition of glycerol.The OpenSPEC software can quantify in real-time changes to the absorbance spectrum.

Surface Plasmon Resonance Analysis of Plasmonic Nanoparticles In Free-Solution with OpenSPR

Metal nanoparticles exhibit unique optical characteristics, and characterization of these properties is essential for the development of next generation biosensors, evaluating new synthesis techniques, understanding the underlying physics and many other applications. In this Application Note, we compare the properties of 1% gold plated silver decahedral nanoparticles to pure silver decahedral nanoparticles. Plasmonic changes due to ligand binding are correlated with structural changes observed using TEM.

Reducing Non-Specific Binding in Surface Plasmon Resonance Experiments

Non-specific binding is an important experimental parameter to control when using SPR systems. Non-specific binding is caused by molecular forces (charge interactions, hydrophobic interactions, etc.) between the analyte and the sensor surface. The effect of non-specific interactions is a false positive contribution to the signal in a sensorgram. It is important for users to recognize non-specific binding and to implement strategies to reduce or eliminate its effects to get accurate kinetic data. The most common methods include the addition of bovine serum albumin (BSA) as a blocking protein, the addition of a surfactant such as Tween 20, careful adjustment of the buffer pH, and the addition of salt.

Gold Nanoparticles for Surface Plasmon Resonance

A major advantage of surface plasmon resonance is that it is label-free, so unlike techniques like ELISA, no label molecule is required to detect the target of interest. However, surface plasmon resonance systems are expensive, typically costing upwards of $100,000, making them inaccessible to the vast majority of scientists and researchers. OpenSPR™ by Nicoya Lifesciences is different— is doesn’t use a planar gold film, prism, or any of the complicated optics you would find in classic surface plasmon resonance systems. Instead, it uses gold nanoparticles to generate what is known as localized surface plasmon resonance (LSPR).

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