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The dots on this image are not stars, but millions of proteins, seen under the microscope. Each protein rises like a blade of grass whose only extremities are visible when we look from above. Proteins are amino acid chains, so every point is just the amino acid of the tip. Among the 20 types of amino acids that make up proteins, one type is labeled yellow, another is pink, the other 18 are not labeled, they are black. By removing an amino acid from each protein, taking a new image and then repeating several times, researchers can record an amino acid sequence for each protein in a sample of millions of people simultaneously. Credit: University of Texas at Austin
A team of researchers from the University of Texas at Austin has demonstrated a new method of protein sequencing much more sensitive than existing technology, by identifying individual protein molecules instead of requiring millions of molecules at a time. This breakthrough could have a major impact on biomedical research, facilitating the discovery of new biomarkers for the diagnosis of cancer and other diseases, as well as improving our understanding of the functioning of healthy cells.
The team published the results of their concept validation study today in the journal Nature Biotechnology.
"We have created, essentially, a DNA sequencing type of technology to study proteins," said Edward Marcotte, professor of molecular bioscience and co-inventor of the new technology.
Work on this project began more than six years ago when Marcotte and his colleagues first considered adapting next-generation gene sequencing methods to protein sequencing. Next-generation gene sequencing is a set of techniques that have been able to sequence the entire genome of any living organism quickly, accurately, and affordably, by accelerating biological research – and for the rest of us, by allowing genetic testing at home for heritage and disease.
In the same way that these earlier advances provided fast and comprehensive information on thousands of genes that influence human health, the new technology provides fast and comprehensive information on tens of thousands of proteins that play a role in healthy or healthy functioning. in diseases. In many disorders, such as cancer, Alzheimer's disease, heart failure and diabetes, cells produce proteins and other substances that act as unique biomarkers, similar to fingerprints. Better detection of these biomarkers would help researchers understand the causes of the disorder or provide earlier and more accurate diagnosis to patients.
A new, ultra-sensitive method of identifying the series of amino acids in individual proteins (eg protein sequencing) can accelerate research on biomarkers of cancer and other diseases. Credit: David Steadman / University of Texas at Austin
The current laboratory standard for protein sequencing, which uses a tool called mass spectrometry, is not sensitive for many applications: it can detect a protein only if there are about one million copies. It also has a "low throughput" meaning that it can detect only a few thousand distinct types of proteins in a single sample.
With this new method, called fluorose-sequencing of a molecule, researchers can now sequence millions of individual protein molecules simultaneously in a single sample. Marcotte thinks that with future improvements, the number of molecules that can be detected in a sample could reach billions. With a higher throughput and much greater sensitivity than existing technology, the tool should enable better detection of biomarkers of the disease and would also investigate such things as cancer of one's own. all new way. For example, researchers could examine, cell by cell, how a tumor evolves from a small mass of identical cells to a soup of genetically divergent cells, each with its strengths and weaknesses. Such knowledge could inspire new ways to fight cancer.
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More information:
Identification by a single highly parallel molecule of proteins in mixtures at zeptomole scale, Nature Biotechnology (2018). DOI: 10.1038 / nbt.4278, https://www.nature.com/articles/nbt.4278
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