CBE Ph.D. Student Vaishnavi Mahankal Wins Best Poster Award at Pittsburgh Diffraction Conference
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Ph.D. student Vaishnavi Mahankal of the UMass Amherst Chemical and Biomolecular Engineering (CBE) Department won the Chung Soo Woo Award for best poster at the Pittsburgh Diffraction Conference encapsulating her groundbreaking research on a "Fixed-Target Microfluidic Device for Anaerobic Crystallography.” The Pittsburgh Diffraction Conference is one of the longest-running scientific meetings in North America focused on the advancement of structural science through diffraction-based methods. Mahankal works in the research lab of Professor Sarah Perry, and her research, in general, focuses on the development of microfluidic platforms for time-resolved protein crystallography.
Mahankal’s poster summarized her research with Perry and collaborators from the University of Michigan Medical School and the Stanford Linear Accelerator Center National Accelerator Laboratory in Menlo Park, California, to work out a crucial problem with understanding protein structure and its functions.
According to the research team’s abstract, “Understanding a protein’s structure, its interactions with other molecules, and its regulatory mechanisms is a key to figure out its role in biology. Structural analysis is important to identify this functional background and also to advance drug discovery, disease modeling, and personalized medicine.”
The abstract points out one key problem that this research addresses: Among the numerous potential protein targets, redox-sensitive metalloproteins, which are involved in key processes of respiration and oxygen transport, are inherently unstable in aerobic environments because oxygen can alter the metal site and/or surrounding protein structure.
“These challenges have resulted in considerable difficulties in elucidating details of the structure-function relationship,” as the team’s abstract says. “Apart from being unstable at ambient conditions, this vulnerability becomes even more pronounced during X-ray-diffraction experiments, where intense radiation from synchrotron sources causes structural alterations that can deviate significantly from the native state.”
The research team says that cryogenic cooling has traditionally been employed to reduce such damage because it slows down radiation-induced reactions and minimizes oxygen diffusion. However, the same mechanisms that slow the effects of radiation damage also prevent direct observation of functional motions within the proteins.
Mahankal’s research focuses on a significant solution. “To overcome these limitations,” she says, "we are developing an anaerobic fixed-target device that will be used for data collection at ambient temperatures.”
As the abstract expounds, “To create a stable anaerobic environment inside the device, we are exploring different types of novel, X-ray-compatible materials such as graphene and Ostemer. Graphene, due to its atomic thinness and impermeability to gases, serves as a key oxygen barrier, while Ostemer is a UV-curable polymer that takes advantage of thiolene click chemistry.”
The research team concludes that “We are validating our approach via colorimetric studies using the redox-sensitive dye methyl viologen, as well as Hemoglobin and Methyl-Coenzyme M Reductase as more challenging protein targets.”
As the Pittsburgh Diffraction Conference website explains about its purpose, “Bridging both life sciences and materials sciences, the conference brings together researchers who utilize laboratory-based instruments, X-ray-light sources, electron diffraction, and neutron scattering to explore the structure and dynamics of matter. It serves as a vibrant forum for sharing recent scientific breakthroughs, fostering interdisciplinary collaborations, and highlighting innovations across experimental and computational frontiers.”