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HomeTechnical Services Biomolecular Interaction
Biomolecular Interaction
Kd/Ka/KD analyzed. Binding affinity quantified.
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ADVANTAGES
Various Types of
Testing Methods
Testing Methods
SPR, ITC, BLI, MST
Cost
Effectiveness
Effectiveness
Free chips and affordable compounds and recombinant proteins
One-Stop
Supply
Supply
Protein purification capability& Compound screening capability
Professional
Instrucments
Instrucments
Biacore, Octet, Nano Temper
SURFACE PLASMON RESONANCE (SPR)
Provided by TargetMol
Principle: Surface Plasmon Resonance (SPR) is an optical phenomenon induced by either photons or electrons. When light is incident from an optically dense medium to an optically sparse medium, total internal reflection occurs, forming an evanescent wave entering the optically sparse medium. The incident angle causing Surface Plasmon Resonance is referred to as the SPR angle. SPR phenomena are related to the refractive index of the metal surface. When an analyte binds to the chip, refractive index alters that causing a change in the SPR angle. Biosensors detect these changes in real-time, allowing the monitoring of molecular interactions. In experiments, one biological molecule is immobilized on the surface of chip, and the molecule interacting with it is dissolved in a solution flowing over the chip surface. The detector tracks the changes in the binding and dissociation of molecules in real-time. Surface Plasmon Resonance (SPR) based on Biacore allow highly sensitive real-time monitoring of interaction between two molecules(including proteins, molecules, DNA, RNA), enabling high-throughput screening. As an innovative biosensing analysis technology, SPR experiments span every stage of drug development, including target discovery, drug screening, proteomics, immunogenicity, biopharmaceutical research and development, production, as well as life science research.
MICROSCALE THERMOPHORESIS(MST)
Principle: Microscale Thermophoresis (MST) bases on the thermophoresis of biomolecules. The nanoTemper MST instrument uses infrared lasers for local heating, causing directional movement of molecules. Subsequently, the distribution of molecules in the temperature gradient field is analyzed through fluorescence. This movement is then analyzed by fluorescence to determine the size, charge, and hydration layer changes of biomolecules due to binding. The MST instrument records fluorescence changes of the sample in the region irradiated by the infrared laser before, during, and after laser opening in a temperature gradient, enabling rapid measurements.
BIOLAYER INTERFEROMETRY (BLI)
Principle: Biolayer Interferometry (BLI) is a technology that detects surface reactions by measuring the displacement of interference spectra. When visible light is emitted from a spectrometer, two sets of reflected spectra are formed at the two interfaces of the optical film layer on the sensor's end, creating an interference spectrum. Changes in layer thickness and density due to molecular binding or dissociation can be reflected by the displacement value of the interference spectrum. In Fortebio Octet BLI experiments, one molecule is immobilized on the sensor surface, and the binding of another molecule causes an interference shift in the sensor, generating real-time binding curves. BLI allows label-free, real-time quantitative testing with accurate, objective, and reliable results.
ISOTHERMAL TITRATIONVCALORIMETRY(ITC)
Principle: Isothermal Titration Calorimetry (ITC) is a technique for quantitatively studying various biomolecular interactions. It directly measures the heat released or absorbed during the binding process of biomolecules. By measuring the heat transfer during the binding process, binding constants (KD), reaction stoichiometry (n), enthalpy (ΔH), and entropy (ΔS) can be accurately determined. The instrument includes a reference cell and a sample cell. During the experiment, the ligand is titrated into the sample cell in a controlled manner (accompanied by thorough mixing). Each titration generates a heat pulse, and by integrating the heat for each titration and normalizing for concentration, the molar heat release (kcal/mol) is obtained. Plotting the molar ratio (ligand/sample) and selecting an appropriate binding model allows the determination of binding-related affinity (KD), stoichiometry of binding (n), enthalpy change (ΔH), and entropy change (ΔS).
DIFFERENTIAL SCANNING FLUORIMETREY (DSF)
Principle: The fluorescence of tryptophan and tyrosine in proteins is closely related to their environment. The label-free nanoDSF technology accurately detects changes in intrinsic fluorescence during protein thermal and chemical denaturation processes. By tracking changes in intrinsic fluorescence, the folding status of the protein can be monitored. The fluorescence signal ratio changes with increasing temperature or concentration of chemical denaturants, allowing the determination of protein stability parameters such as the Tm value. DSF achieves the detection of protein thermal or chemical stability in a label-free environment.
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