Release Date: September 10, 2013
BUFFALO, N.Y. – Thanks to efforts like the Human Genome Project, scientists are unraveling the role that genes play in the development of diseases such as cancer and Alzheimer’s.
But knowledge of proteins, another essential molecule linked to many of the same ailments, is less advanced.
That is changing due in part to UB researcher Sheldon Park, who received a $300,000 National Science Foundation grant to develop technology that dramatically reduces the time it takes to characterize proteins.
“We are creating a method that allows scientists to examine what role proteins play in the cell. Typically, this type of research takes months to perform. Now, it can be done it just a few days,” said Park, UB assistant professor of chemical and biological engineering.
The breakthrough technology could be useful in proteomics, a field of study which examines how proteins function in the cell. In what many see as the next step after sequencing the human genome, proteomics aims to create a functional description of the human body’s estimated million or so unique proteins.
By examining this data, scientists may find clues as to why cancer, Parkinson’s Disease and other ailments develop. It could lead to the development of drugs and other treatments, and possibly even a cure for the diseases.
Until recently, however, such research didn’t seem possible.
The human body consists of roughly 21,000 genes, each of which can spawn proteins of different size and function. Given the complexity of the protein network, it has been difficult to characterize what proteins do despite efforts from pharmaceutical companies, government agencies and research institutes.
Researchers often study proteins by creating temperature-sensitive mutant proteins which work like the original proteins at low temperatures but stop working at higher temperatures. By comparing the growth and metabolism of cells at different temperature, scientists can determine the mutated protein’s function.
The problem: creating temperature sensitive mutants is not easy and often impossible. Typically, researchers must screen a few thousand mutants. With some luck, they may discover a useful one. This painstaking process can take months and it needs to be repeated for each protein studied.
“It’s a very laborious process and, unfortunately, not very predictable,” Park said.
To simplify the matter, he is designing a module that, when fused to a protein, converts the protein into a temperature sensitive mutant. A key element of the design is an enzyme called intein, which can be used to shuttle the protein to different areas of the cell by changes in temperature. As the protein moves from one area of the cell to another, scientists are able to infer its function by examining what happens in the cell.
The technology has the potential for wide use in chemical research, biotechnology, medicine and other fields.
“The grant will also allow us to develop a method that uses an engineered intein to synthesize useful protein molecules in the lab,” Park said. “In turn, this will give researchers the ability to gather information about unknown proteins and develop novel treatments or biotechnology applications.
“Understanding the functions of proteins will have
significant impact on the diagnosis and treatment of illnesses
caused by mutations,” he said.
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