* Please be kindly noted that our services and products can only be used for research to organizations or companies and not intended for any clinical or individuals.
The structural analysis of target proteins and ligands is a very important component in PROTAC design. With senior high-level scientists and experienced chemical structural optimization platform, BOC Sciences provide the service in a customizable fashion to suit our customers' specific research goals. Please do not hesitate to contact us for more details about our protein-ligand structural analysis services.
A PROTAC molecule consists of two key domains: a domain that binds specifically to the target protein to be degraded, and a domain that binds to E3 ubiquitin ligase (E3 ligase), which are connected by a specific linker (linker). Protein-ligand and protein-protein interactions play a fundamental role in PROTAC drug discovery. A number of computational methods have been developed to characterize and use the knowledge of this interaction, which can lead to drug candidates and eventually produce compounds in the clinic.
The specific molecular interactions of biological macromolecules with different sizes of ligands are essential for understanding the regulation of key cellular processes. Proteins are the most important class of biological macromolecules because they control the key structural and functional properties of the cell system. To well understand the molecular mechanisms behind important cellular processes, it is clear that it is necessary to examine the structural interactions of proteins with themselves or with other biological macromolecules, such as nucleic acids, polysaccharides and lipids. Due to the core role of protein as the driving force of cell function, the specific interaction between small molecular organic ligands and proteins is very important for reasonable drug design. Some biophysical and biochemical techniques, such as isothermal titration, surface plasmon resonance, fluorescence resonance energy transfer, infrared spectroscopy, circular dichroism, confocal microscopy and enzyme-linked immunosorbent assay, have been successfully used to characterize the binding constant (KD), kinetics, kinetics and thermodynamics of protein-ligand interaction.
We provide a commonly used analytical technique that can be used to study different aspects of the interaction between proteins and small molecular organic ligands.