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High resolution 3D structures of proteins or protein-complexes
Cryo-EM has become a standard structural technique for structural determination of proteins and protein-complexes, especially for samples that limit the use for X-ray crystallography and NMR due to size, crystallization difficulty, stability, complexity and conformational variability. High resolution 3D structures of proteins and protein-complexes provide scientist with deeper understanding of biological processes, mechanisms of action of molecules, and structure-activity relationships, which can enlighten all steps of drug discovery.
3D structure determination and characterization of small molecule using cryo-EM can assist optimization of chemical synthesis, understanding of structure-activity relationship. It can also guide the design of formulation and drug delivery approach. Use of microcrystal electron diffraction (micro-ED) on small molecules serves as a better solution when NMR can only provide unclear result or X-ray crystallography is time consuming or not feasible.
Cryo-EM is an effective technique to map the interactions between antibodies and antigens and has many applications in antibody development and biologics discovery. Structural data can be used for paratopes/epitopes identification, correlation between structures and activity, identification of cross-specificity, monoclonal antibody (MAB) optimization and IP protection. High-resolution structures showing interaction between antibodies and antigen can also be applied to guide vaccine development as an alternative to the traditional approach.
By providing high-resolution structural information, cryo-EM can support development and manufacturing programs for the design of new drug delivery systems by characterizing shape, size and size distribution, morphology of different samples such as nanoparticles, , liposomes, Adeno Associated-Virus (AAV) and other viral like particles. These techniques has been acknowledged as a standard quality control approach in many manufacturing scenarios.
Proteolysis targeting chimera (PROTAC) technique has drawn great attention due to its potential to target “undruggable ”proteins by linking two small-molecule binding ligands. Structural information of binding mechanism of small molecule and targeted protein or E3 ligase can significantly improve the understanding of PROTAC technique. By using cryo-EM, it is possible to visualize such binding interaction and provide insight for molecule design and searching new binding sites on targeted protein.
Shuimu BioSciences Ltd.
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