$300K awarded to Colorado scientist developing new treatments

Research on synthetic 'scaffolds' to disrupt toxic clumping of alpha-synuclein

Lindsey Shapiro, PhD avatar

by Lindsey Shapiro, PhD |

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A research lab at the University of Denver in Colorado has received $300,000 in funding from the Parkinson’s Foundation to develop and test potential treatments for Parkinson’s disease.

The Foundation’s Stanley Fahn Junior Faculty Award was granted to Sunil Kumar, PhD, an assistant professor of molecular and cellular biophysics at the university, who is now the first researcher in Colorado to receive the honor.

Three researchers in North America are tapped for the award annually based on their promising, early career research. In addition to three years of financial support, winners have an opportunity to participate in the Foundation’s annual summit in Washington, D.C., and to receive feedback from the Foundation about their research project.

“They see a real potential in it,” Kumar said in a university news story. “The award will be extremely helpful in continuing this work and the reviews for it were really nice.”

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Toxic alpha-synuclein clumping implicated in Parkinson’s

Kumar’s lab is working on developing synthetic molecules called scaffolds or foldamers that will disrupt the toxic clumping (aggregation) of the alpha-synuclein protein in Parkinson’s. The accumulation of a misfolded version of alpha-synuclein is thought to underlie the death of nerve cells that drives Parkinson’s symptoms.

Essentially, the lab-made scaffolds would be designed to bind to the spot on alpha-synuclein that’s necessary for initiating its aggregation, thus preventing the process.

Other labs have tried a similar approach using peptides, or short protein chains, but the approach hasn’t been as successful as the synthetic molecules, according to the researcher.

“Peptides are often chewed up by the machinery in our bodies,” Kumar said, noting that the synthetic molecules are not as susceptible to this. “These molecules don’t get chewed up and they mimic the structures of those proteins.”

In a previous study published in Nature Communications, Kumar’s team identified the protein sequence on alpha-synuclein that initiates aggregation. They then designed a scaffold that would interrupt that interaction and block alpha-synuclein buildup.

The molecule was found to prevent aggregation in cell culture models of Parkinson’s as well as in post-mortem brain tissue from Parkinson’s patients. In a worm model of the neurodegenerative disease, treatment with the scaffold was also found to increase locomotor activity, which is usually diminished in the model.

“In a person with Parkinson’s, a protein will come along and bind, then another and another,” Kumar noted. “Our molecules stop that. It looks like the same protein and sort of tricks the body, so it won’t keep on building clumps.”

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Potential to treat other neurodegenerative diseases

The scientist also believes there is potential to apply these scaffolds for the treatment of other neurodegenerative diseases, such as amyotrophic lateral sclerosis, or possibly some cancers.

“There’s some really cool data and a lot of opportunity,” he noted.

Kumar credits the undergraduate and graduate students in his lab who have helped conduct the studies. One student has also been awarded a fellowship from the Parkinson’s Foundation to contribute to the research.

“We’ve been able to incorporate the work of a lot of students at different levels,” Kumar said. “We work really hard, but it’s a collaborative environment.”