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Oncological imaging and structural analysis guide cancer research
Cryo-electron microscopy (cryo-EM) is continuing to revolutionize our understanding of cancer and cancer treatments through high-resolution imaging of oncology targets. Scientists have used single particle analysis to uncover new cancer pathways, obtain atomic-level descriptions of key cancer proteins, and provide a framework for improving pharmaceutical interventions.
Genomic integrity and cell growth regulation lie at the heart of cancer, and proteins play a large role in mediating these mechanisms. Cryo-EM can freeze biomolecules in their native conformations and visualize protein interactions, capturing different stages of biochemical reactions beyond just pre-reaction and end states. With such structural insights, researchers can better understand the conditions required for cancer cell growth and identify new ways to treat cancer through structure-based drug discovery.
Structural biology techniques for oncology research and therapeutic development
Cryo-EM has become an invaluable tool in characterizing protein structures and identifying how they behave as part of key cellular functions and mechanisms. Such advanced oncological imaging provides insights into the molecular mechanisms of cancer and facilitates the development of targeted therapies. Below are just a few frequently asked questions on how structural biology and cryo-EM can support oncological research and drug development; for more information, do not hesitate to contact us.
To improve our understanding of cancer pathways, structural biologists focus on the structures of proteins, active sites, and protein-protein interactions. This information can support the development of targeted cancer therapies for pharmaceutical intervention.
X-ray crystallography, NMR spectroscopy, and cryo-EM techniques have been used to study protein structures.
Single particle analysis, a cryo-EM technique, can be used to characterize protein structures at high resolutions without the need for crystallization. In cryo-EM, samples are frozen in amorphous (vitreous) ice, which maintains molecular structures, conformations, and interactions in their natural state. This allows researchers to capture multiple phases of proteins and even intermediate protein interactions. Additionally, cryo-EM can be used to visualize molecules that are difficult to observe with other structural biology techniques, such as membrane proteins, which can be challenging to crystallize for X-ray crystallography.
Structural insights from techniques like cryo-EM can support oncological drug discovery and development through the identification of targets and molecular mechanisms. This can guide the design of drugs that bind to specific target sites or the further refining of existing interactions with target molecules.
Cryo-EM resources for cancer research
For Research Use Only. Not for use in diagnostic procedures.