CD BioSciences is committed to developing a variety of technologies such as isothermal titration calorimetry (ITC) to provide customers with thermodynamic measurements of biomolecular interactions. Our detailed and integrated thermodynamic characterization services will make an important contribution to our customers in understanding and optimizing molecular interactions.

Background

In the field of drug discovery, the term "thermodynamics" refers to the study of the thermal changes that occur when molecules interact with each other. Thermodynamic characterization of such temperature changes plays an important role in the drug design and development process. With the continuous development of our understanding of the energy basis of molecular interaction, thermodynamic characterization methods have also made significant progress, accelerating the thermodynamic driven drug design.

Comprehensive thermodynamic characterization can provide information on the energy balance driving binding interactions, which is essential for accelerating drug development to achieve optimal energy interaction profiles while maintaining good pharmacological properties. ITC is currently one of the most commonly used techniques for the quantitative study of various biomolecular interactions. The general applicability of ITC and the exceptionally low error in affinity measurements commonly observed with this technique make it the gold standard for measuring binding parameters.

Fig.1 Examples of ITC data for complex interactions. (O'Brien, 2017)

Our Technology Platform

We offer ITC to measure the thermodynamic data directly, or indirectly through other methods that can be used to determine the K_D as a function of temperatures, such as surface plasmon resonance (SPR) or fluorescence. In addition, we also offer higher throughput thermodynamic measurements to meet the needs of our customers for high throughput drug screening methods, including high throughput thermal shift analysis and high throughput calorimetry.

Our Services

We offer a variety of strategies to provide our clients with the thermodynamic characterization of biomolecular interactions. Our services include but are not limited to:

• Real-time monitoring of protein/protein interactions, as well as protein/small analyte interactions during secondary screening, lead optimization and selection.
• Thermodynamic characterization of ligand-target binding. We help our customers measure the heat transfer during binding and accurately determine the affinity (K_D), stoichiometry (N), enthalpy (∆H) and entropy (∆S), providing complete thermodynamic information on molecular interactions.
• Determine the kinetic parameters associated with protein-ligand recognition.

Applications

Our thermodynamic characterization services can be widely used in the following aspects of drug discovery and development:

• Quantifying binding affinities.
• Selection and optimization of drug candidates.
• Characterization of biomolecular interaction mechanisms.
• Identifying prospective binding targets in the small molecule drug discovery process.
• Determination of binding specificity and stoichiometry.
• Enzyme kinetic assays.

Equipped with an advanced biotechnology platform, CD BioSciences offers clients a detailed thermodynamic characterization service for biomolecular interactions. If you are interested in our services, please contact us for more details.

Reference

1. O'Brien, R.; et al. Thermodynamics in drug discovery. Applied biophysics for drug discovery. 2017: 7-28.

• Drug Design Based on X-ray Crystallography
• Target Binding Analysis by HDX-MS
• Binding Affinity Measurement by MST
• Protein Stability Evaluation by TSA
• Fragment Screening Based on WAC
• Hit Identification by NMR-based Techniques
• Qualification of Targeting Protein-Protein Interactions
• Measurement of Ligand Binding Kinetics
• Identification of Small-Molecule Aggregation
• Analysis of Free Energy Calculations
• Modeling of Scaffold Hopping Transformations
• Cellular Imaging Service for Drug Discovery
• AFM-Based Biophysical Analysis of Drugs