Proteins function in a variety of ways in biological systems, such as signaling molecules, structural elements, catalysts, and receptors. Small chemicals called ligands have the ability to specifically connect to proteins and modify their function, which triggers physiological reactions.
Creative Proteomics offers a state-of-the-art technology platform for protein-ligand interaction analysis. Leveraging cutting-edge techniques and expertise, Creative Proteomics empowers researchers to unravel the complexities of molecular recognition. Let's explore some key components of their technology platform:
MicroScale Thermophoresis (MST) is a powerful biophysical method employed by Creative Proteomics for protein-ligand interaction analysis. This technique allows for the measurement of binding affinities and thermodynamic parameters by monitoring the movement of fluorescently labeled proteins in response to ligand binding. MST provides exceptional sensitivity, high reproducibility, and the ability to work with low sample volumes. By employing MST, Creative Proteomics enables precise characterization of protein-ligand interactions, aiding in the identification and optimization of lead compounds.
Creative Proteomics utilizes nano-Differential Scanning Fluorimetry (nanoDSF) to study protein-ligand interactions and assess protein stability upon ligand binding. This technique measures changes in the fluorescence emission of a thermally sensitive dye as the protein-fragment mixture undergoes a thermal ramp. By analyzing the thermal stability and conformational changes induced by ligand binding, nanoDSF provides valuable insights into the binding affinity and ligand-induced effects on protein stability. This information guides the optimization of lead compounds and facilitates structure-activity relationship studies.
Surface Plasmon Resonance (SPR) is a label-free optical technique that enables real-time monitoring of biomolecular interactions. Creative Proteomics employs SPR technology to investigate protein-ligand interactions, measuring binding kinetics and affinity. By immobilizing the target protein on a sensor chip, ligand binding events can be detected and quantified, providing valuable data for hit validation and lead optimization.
Isothermal Titration Calorimetry (ITC) is a powerful technique for studying protein-ligand interactions in a label-free manner. Creative Proteomics utilizes ITC to measure the heat changes that occur during the binding of a ligand to its target protein. By determining the thermodynamic parameters of binding, such as the binding constant (Kd) and enthalpy change (ΔH), ITC provides insights into the affinity and energetics of protein-ligand interactions.
X-ray crystallography is a widely adopted technique for determining the three-dimensional structure of proteins and their complexes with ligands. Creative Proteomics employs X-ray crystallography to elucidate the atomic-level details of protein-ligand interactions, unveiling the precise binding mode, key interactions, and potential areas for optimization. This structural information serves as a cornerstone for rational drug design.
Nuclear Magnetic Resonance (NMR) spectroscopy offers a powerful tool for studying protein-ligand interactions in solution. Creative Proteomics utilizes NMR spectroscopy to investigate dynamic changes, conformational alterations, and binding kinetics of proteins upon ligand binding. Through techniques such as Saturation Transfer Difference NMR (STD-NMR) and Structure-Activity Relationship by NMR (SAR by NMR), researchers can gain invaluable insights into ligand binding and guide optimization efforts.
Computational modeling and docking studies play a pivotal role in protein-ligand interaction analysis. Creative Proteomics employs advanced computational techniques to predict and model protein-ligand complexes, allowing for virtual screening, binding affinity estimation, and optimization of lead compounds. These computational tools complement experimental methods and aid in the rational design of novel therapeutics.
GPCR binding assays focus on the interaction between G protein-coupled receptors (GPCRs) and ligands, a diverse class of membrane proteins that play a key role in cellular signaling and are involved in many physiological processes.Creative Proteomics uses advanced technologies and assays to assess the binding affinity, kinetics and selectivity of ligands for specific GPCRs, providing scientific insights into ligand-receptor interactions, kinetics and selectivity of specific GPCRs, providing scientific insights into ligand-receptor interactions.
The core of kinase binding assays is the study of the interaction between kinases and ligands. Kinases are a class of enzymes that regulate cellular signaling pathways that are commonly dysregulated in a variety of diseases, including cancer. Using our expertise in kinase assays, we assess the binding affinity, selectivity and potency of ligands for specific kinases.
Fragment-based drug discovery interaction analysis is used to identify lead compounds with desirable drug-like properties. By employing high-throughput screening techniques, we can efficiently assess fragment-protein interactions, determine hit rates, and guide the subsequent optimization process. This analysis plays a key role in the development of effective and selective drug candidates.