Revolutionizing Protein Imaging: A Game-Changer in Drug Discovery
Unveiling the Era of Miniature Protein Imaging
A groundbreaking advancement in the field of biochemistry has been made by a team of researchers from UCLA, in collaboration with scientists from the pharmaceutical industry. This advancement pertains to the field of cryo-electron microscopy (cryo-EM), a technique that won the Nobel Prize in 2017. The researchers have developed a method that allows for the imaging of smaller protein molecules, a feat previously unaccomplished as cryo-EM was limited to the imaging of larger molecules.
The Innovation: A Cube-Shaped Protein Scaffold
The novel innovation involves the creation of a cube-shaped protein structure, or scaffold, measuring 20 nanometers. The scaffold is designed with rigid, tripod-like protrusions that hold small proteins in place. This scaffold can be digitally removed during image processing, resulting in a high-quality 3D image of the small protein being analyzed.
Significance of the Advancement
This groundbreaking research holds considerable importance as small and medium-sized proteins are a pivotal area of focus in the search for potential new drugs for diseases such as cancer. The advancement was put to the test on a protein that is currently being studied for its potential use in cancer treatments. The method can be customized for almost any small protein, and it is anticipated to assist researchers in identifying specific locations on proteins that can be targeted for therapeutic purposes.
The Process of Cryo-Electron Microscopy
Cryo-EM involves sending a beam of electrons through frozen samples of material, leaving behind an image of the thousands of molecules in the sample. The molecules are imaged exactly as they are in the sample, resulting in thousands of 2D photographs of the molecule from different angles. These photographs are then processed by a computer to create a high-resolution 3D image. However, the small size of some protein molecules makes it challenging to accurately determine their orientations in the images, leading to relatively low-resolution images.
Observing the Atomic Structure of KRAS
The UCLA-led team was successful in observing the atomic structure of a protein called KRAS, which is involved in about 25% of human cancers. Using cryo-EM and the new scaffold, the team was able to see how a drug molecule, being studied as a potential treatment for lung cancer, binds with and inhibits KRAS. This could potentially guide the development of more effective drugs.
Collaborative Effort and Future Potential
The research was supported by the National Institutes of Health and was a collaborative effort with scientists from Astra-Zeneca and Gandeeva Therapeutics. UCLA has filed a patent for the new technology, and the researchers have started a new company, AvimerBio, to develop commercial applications for the new methodology in collaboration with leading pharmaceutical companies.
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