Molecular Interactions

service

Structural Biology

  Tel:18962587269
  Email:contact@readcrystal.com
  Address:Changshu High-tech Industrial Development district, Suzhou, Jiangsu Province 1001, Building 6, No.88 Xian Shi Road

      Molecular interactions include nucleic acid-nucleic acid interactions, nucleic acid-protein interactions and protein-protein interactions. Molecular interaction experiments enable visual interpretation of biological processes and molecular recognition processes, and elucidate the mechanisms of action between molecules, validate the ability of drug candidates to bind to target molecules, drive the discovery of drug leads and optimize the safety, efficacy, dosage form and manufacturing process of drugs.

      ReadCrystal establishes a team of molecular interactions with extensive experience, providing a full range of service from protocol design to technical implementation for nucleic acid-nucleic acid, nucleic acid-protein and protein-protein interactions.

Isothermal Titration Calorimetry(ITC)
Experimental principles

At a set stable reaction temperature, when a macromolecule/ligand conjugate is generated, the release or absorption of energy results in a change in cuvette temperature which is precisely detected and recorded. Typically, a complete ITC experiment involves determining reactant concentrations, titrating, collecting data, calibrating the raw data, deriving thermodynamic parameters from the calibrated data and analyzing the model.

Applications
•   Quantifying binding affinity
•   Selection and optimization of drug candidates
•   Determination of thermodynamic properties and activity concentrations
•   Characterisation of mechanism
•   Identifying prospective binding targets in the small molecule drug discovery process
•   Determination of binding specificity and stoichiometry
•   Validation of IC50 and EC50 values during the evolution from seedling compound to lead compound
•   Enzyme kinetic assays
Technical features
•   No restrictions on the system being studied
•   Small sample size, high sensitivity accuracy
•   Short test time
•   Marker-free test
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Surface Plasmon Resonance(SPR)
Experimental principles
Surface plasmon resonance is an optical phenomenon that monitors the interaction process between various types of biomolecules via SPR sensing chips under conditions without fluorescence or isotope labelling. It follows the whole process of binding and dissociation between the solution and the molecules on the surface of the chip, and captures various specific signals during the experiment, which are finally integrated by data analysis software into interactions kinetic parameter data. Due to its high degree of automation, high sensitivity and dynamic monitoring characteristics, it is now widely used in the study of the interaction mechanisms of various biological molecules.
Applications
•   Small molecule drug-protein interactions
•   Antigen-antibody interactions, biologics development
•   New drug development: drug-monolayer cell interactions
•   Single-chain antibody binding kinetics
•   Single-chain oligonucleotide quantification
•   Targeted drug transport studies
Technical Features
•   Marker-free testing process
•   High throughput testing, up to 8 channels
•   High sensitivity, typically for compounds down to molecular weight at 100
•   Low sample usage
•   Real-time detection
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 Micro-Scale Thermophoresis (MST)
Experimental principles
Micro-Scale Thermophoresis is an optical method for characterizing biomolecules by observing the movement of particles across a microscopic temperature gradient (usually through a 1480 nm infrared laser, irradiated to the sample after a dichroic mirror. This process creates a temperature gradient as water molecules absorb infrared light and heat up) to analyze intermolecular interactions and various chemical dosimetry parameters.
Applications
•   Protein-small molecule interactions (protease-inhibitor interactions, cell membrane protein activity analysis)
•   Protein-peptide interactions
•   Protein-protein interactions
•   Peptide-peptide interactions
•   Protein-nucleic acid interactions
•   Nucleic acid aptamer-small molecule interactions
Technical features
•   Low sample consumption
•   No sample fixation, no purification required
•   Short measurement times
•   High sample compatibility
•   Combined in complex buffers for analysis
•   Study of multi-component reactions
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 Differential scanning fluorimetry(DSF)
Experimental principles

This technique is used for high throughput drug and target screening by measuring the thermal stability of proteins. DSF uses special fluorescent dyes as indicators, which bind and enhance fluorescence when the protein folding structure changes at elevated temperatures.

Applications
•   High throughput drug screening and target discovery
•   Protein stability
•   High-throughput screening of protein stabilizers and inhibitors
•   Protein mechanism of action studies
•   Small molecule inhibitor mechanisms
•   Protein structure studies

Molecular Interaction

•   Low sample loss
•   High throughput
•   Wide range of temperature variation
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Nano Differential Scanning Fluorimetry (nano-DSF)
Experimental principles
The fluorescence of tryptophan and tyrosine in proteins can vary with the environment. Nano-DSF technology can accurately detect changes in endogenous fluorescence during thermal and chemical deformation of proteins to track their folding state and determine protein stability parameters Tm or Cm.
Applications
•   Validating the functionality and long-term stability of biologics
•   Protein formulation screening
•   dentification of biosimilar candidates
•   High throughput screening for enzyme stability
•   Screening of membrane protein detergents
•   Protein quality control
•   Ligand binding assays

Technical Features
•   Samples do not need to be fixed
•   Testing under natural conditions
•   Freedom choice of throughput
•   low sample consumption
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