Matt Shoulders, associate professor in the Department of Chemistry, MIT is trying to understand how protein folding happens in human cells. In order to find ways to prevent diseases linked to protein misfolding.
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Cracking mystery of Potein folding can cure many genetic diseases
Protein Folding is a vital process of the body in order to maintain the proper functioning of the cell. Most of the diseases corresponding to genetic disorders like cystic fibrosis and brittle bone disease, and neurodegenerative diseases like Alzheimer’s, are mainly linked to defects in this protein folding process.
Hence to know the root cause of disease it is important to know why does protein misfold in its process. It is important to analyse the factors and causes that misleads protein in its function.
Matt Shoulders, a recently tenured associate professor in the Department of Chemistry, MIT is trying to understand how protein folding happens in human cells. He also trying hard to know how does protein misfold in order to find ways to prevent diseases linked to protein misfolding.
Let us know more about proteins. Initially, when proteins are made in our cells, they often exist as floppy chains until specialized cellular machinery helps them fold into the right shapes. Only after achieving this correct structure can most proteins perform their biological functions. When there is deviation in protein folding it leads to abnormality and hence mysterious diseases.
“In the human cell, there are tens of thousands of proteins. The vast majority of proteins must eventually attain some well-defined three-dimensional structure to carry out their functions,” Shoulders says. “Protein misfolding and protein aggregation happens a lot, even in healthy cells. My research group’s interest is in how cells get proteins folded into a functional conformation, in the right place and at the right time, so they can stay healthy.”
“Proteostasis is exceedingly important. If it breaks down, you get the disease,” he says. “There’s this whole system in cells that helps client proteins get to the shapes they need to get to, and if folding fails the system responds to try and address the problem. If it can’t be solved, the network actively works to dispose of misfolded or aggregated client proteins.”
To know more about protein folding process Shoulders in his lab at MIT uses a variety of techniques to study the “proteostasis network,” which comprises about a thousand components that cooperate to enable cells to maintain proteins in the right conformations.
According to shoulders to know more about protein folding one must have experience in devising ways to synthesize complex new molecules, including stable peptides that mimic protein functions. Also, protein biophysics plays a role which focuses on the physical and chemical factors that control which structure a given protein adopts and how stable the structure is.
Shoulders have analyzed how proteins fold while in a solution in a test tube. Also, he delving into how proteins fold in their natural environment: living cells.
Neurodegenerative diseases like Alzheimer’s and Parkinson’s diseases are perhaps the best-known protein misfolding disorders, but there are thousands of others, most of which affect smaller numbers of people. Kelly, Wiseman, and many others, including the late MIT biology professor Susan Lindquist, have shown that protein misfolding is linked to cellular signalling pathways involved in stress responses.
“When protein folding goes awry, these signalling pathways recognize it and try to fix the problem. If they succeed, then all is well, but if they fail, that almost always leads to disease,” Shoulders says.
Shoulders and his students have developed a number of chemical and genetic techniques for first perturbing different aspects of the proteostasis network and then observing how protein folding is affected.
Another milestone of shoulders lab is exploring how cells fold collagen. Collagen is the most abundant protein of the human body comprising of more than 4000 amino acids. It is an important component of connective tissue. Collagen misfolding leads to disease and there are about 50 diseases linked to disruption of collagen folding.
Another major concern is the evolution of proteins, especially viral proteins. Flu viruses rapid evaluation is basically due to its ability to hijack some components of the proteostasis network of the host cells they infect. Without this help, flu viruses can’t adapt nearly as rapidly.
Recently Coronavirus created an havoc in china claiming 1000’s of lives. But to everyone concern was how did the virus penetrate the human cells?
And according to scientists, it is the mutation that happened along with their evolution progress. The microscope images of coronavirus show that some cells are attacked by this virus and in turn, these cells go and attack another group of cells.
Know more Coronavirus image Captured
“You might not need one drug for each disease — you might be able to develop one drug that treats many different diseases. It’s a little speculative right now. We still need to learn much more about the basics of the proteostasis network function, but there is a lot of promise.”
-Matthew D. Shoulders, Whitehead Career Development Associate Professor
In the long term, Shoulders hopes that his research will help to identify possible new ways to treat diseases that arise from aberrant protein folding. In theory, restoring the function of a single protein involved in folding could help with a variety of diseases linked to misfolding.
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