Collin Borcik, a postdoctoral researcher in the Rienstra Lab, received the 2024-25 Boyer Award for Postdoctoral Excellence in Biochemistry. The award is presented annually by the Department of Biochemistry to a postdoctoral researcher in recognition of their excellence in research. The award was made possible by Professor Paul D. Boyer, who earned a Ph.D. (1943) from the department.
“I am very honored to receive this award and be part of the great research legacy of UW–Madison and the Department of Biochemistry,” says Borcik. “There are so many outstanding postdocs here, and I am humbled that my research and contributions have been recognized in this way.”
Borcik’s research seeks to determine unique fibril morphologies associated with specific types of Parkinson’s disease, including Lewy body dementia, which could serve as diagnostic markers. Alpha-synuclein — a protein found in the human central nervous system — aggregates to form fibrils which are a diagnostic hallmark in several neurodegenerative diseases, including Parkinson’s disease. Targeting these fibrils could aid in diagnosis and treatment of Parkinson’s disease before the onset of symptoms or early in the illness’s progression, leading to better outcomes for patients.
“We’re getting better at diagnosing Parkinson’s disease, but in the very early stages of disease, symptoms of cognitive decline in different types of Parkinson’s and Alzheimer’s diseases can look very similar, while the underlying causes are different,” explains Borcik. “This makes effective treatment contingent on knowing early on which disease is responsible for the symptoms.”
For these reasons, Borcik says, diagnostic markers that can diagnose Parkinson’s disease before the onset of symptoms or early in the illness’s progression are also key to improving outcomes for patients.
To explore fibril structures, Borcik uses multiple imaging techniques, including solid state nuclear magnetic resonance (ssNMR) and cryo-electron microscopy (cryo-EM). Borcik and collaborators in the Rienstra Lab have developed a software called OPTO to automate adjustments to NMR conditions to boost signal-to-noise in their data, as described in an upcoming publication in the Journal of the American Chemical Society. This optimization, combined with a new NMR probe design that Borcik has also developed, enhances NMR’s ability to identify both strong and weak interactions within a sample, leading to faster data collection and higher sensitivity data for structure calculations.
“Collin has been an exceptional postdoc, exemplifying the spirit of community and scientific excellence that Paul Boyer envisioned when he donated a part of his Nobel Prize to establish this award fund,” says Rienstra. “Collin has not only done exceptional work individually, but he has been an exemplary member of the Department of Biochemistry, strengthening existing collaborations and establishing new ones as a result of his curiosity, collegiality, and persistence.”
One of these collaborations, with the Wright Lab, has resulted in novel approaches to combining information from both NMR and cryo-EM data. This has given Borcik a detailed understanding of fibril structure and how specific binding sites in the fibril proteins interact with ligands used in PET imaging, which can be engineered to help identify Parkinson’s disease in its early stages.
Borcik sees potential for his work on Parkinson’s disease detection to impact the therapeutic field for neurodegenerative disorders. His interest in this work, however, stems in part from personal experience. “This research has the potential to help a lot of people. Not just people with Parkinson’s disease, but their families as well. I speak as someone who lost family members to both Parkinson’s disease and Alzheimer’s disease. Any additional time that families can have together is gold. I hope my research helps to give people a few more good years to spend with loved ones. That’s really what’s important.”