In the News
The 80,000 square foot Physical Sciences Building (PSB) is now open! It provides space for 80 chemistry graduate students and postdocs in 22,000 square feet of state-of-the-art synthetic chemistry labs on Levels 1 and 2, and specialized, “high bay” space for physics on the lower floor. The PSB will be home to 6-8 chemistry research groups, including the Andrew, Kittilstved, Thayumanavan, and Venkataraman groups, who have just moved in (August 2018), as well as new faculty hires.
The building was designed by Wilson Architects and construction was managed by Whiting-Turner. Enhancing collaboration between groups and within a group was a major design goal, as was creating efficient use of space with the flexibility to be readily adapted to meet evolving research needs. The labs feature an open floor plan, so lab space for one group is adjacent to that of another, with no walls between them. In addition to the clear advantages of increasing interactions between groups, this provides the ability for the amount of lab space each group uses to broadly follow changes in group size.
The PSB incorporates numerous green building features and has earned Silver LEED (Leadership in Energy and Environmental Design) certification, which is very challenging for a building with such high air-handling requirements. The extensive windows and glass wall allow natural light to illuminate the labs. Energy-and water-saving features include high-efficiency fume hoods with a hood monitoring system to encourage closing of hood sashes when not in use and a closed-cycle chilled water loop (for stills, etc.). There is open space for specialized instrumentation like glove boxes, and dedicated rooms for high hazard work, solvent dispensing, and mammalian and bacterial cell culture.
Materials scientist Trisha Andrew, computer scientist Deepak Ganesan, and computer engineer Jeremy Gummeson, all part of UMass Amherst’s Institute of Applied Life Sciences’ Center for Personalized Health Monitoring, recently received a three-year, $1.1 million grant from the National Science Foundation’s Computer Systems Research program to advance so-called “smart textiles.”
The next generation of wearable activity sensors will not be strap-on devices that can be lost or forgotten, say researchers at the University of Massachusetts Amherst, instead they may be threads or fabric patches sewn into shirts and pants to offer light, care-free, continuous monitoring of movement that could help doctors, therapists and coaches respond to changes that warrant concern or improve performance.
Professor Scott Auerbach from the Chemistry Department at UMass Amherst, and Professor Wei Fan from the Chemical Engineering Department, also at UMass Amherst, are combining and integrating their expertise in experimental and computational zeolite science, to shed new and important light on how zeolites self-assemble in solution, opening the door to more rational procedures for making new zeolites with advanced performance. Zeolites are the most used catalysts by weight on earth and offer the potential for 21st-century applications in carbon dioxide capture, biofuel production, and nano-electronics. Auerbach and Fan will be awarded a $630,000 grant from the Department of Energy, Basic Energy Sciences in search of the “missing link” of zeolite crystallization.
Catalysts are materials that can steer chemical reactions to the most useful products, and are responsible for society’s affordable access to plastics, fuels, and other materials. Zeolites revolutionized the refining of petroleum in the 1960s and remain essential to this process today. In addition, zeolites show promise for converting chemicals derived from renewable biomass into biofuels. Realizing this promise requires the ability to synthesize zeolites that are tailor-made for specific applications, which in turn requires much better understanding of how zeolite crystals form -- gaining such understanding is the main objective of Auerbach's and Fan's DOE project.
Computational biophysicists are not used to making discoveries, says Jianhan Chen, Professor of Chemistry and Biochemistry & Molecular Biology, so when he and colleagues cracked the secret of how cells regulate Big Potassium (BK) channels, they thought it must be a computational artifact. But after many simulations and tests, they convinced themselves that they have identified the BK gating mechanism that had eluded science for many years.
BK channels are important in neuronal and muscle functions and are associated with pathogenesis of hypertension, autism, epilepsy, stoke, asthma, etc. A key puzzle has been trying to understand how cells close, or gate, BK channels, which have an unusually large central pore. “There were a lot of hypotheses, but no answers,” Chen notes. Now in Nature Communications, his team demonstrates that a phenomenon known as “hydrophobic dewetting” gives rise to a vapor phase in the pore’s central cavity to block intracellular access to the selectivity filter.
Chen’s work on BK channels has also led to a new four-year, $2.9 million grant from NIH’s National Heart, Lung, and Blood Institute. The collaborative team includes Jianmin Cui at Washington University, St. Louis, Chen at UMass Amherst and Xiaoqin Zou at the University of Missouri.
The Martin lab studies the enzyme used by thousands of researches for synthesizing RNA in the test tube. New work published in the journal Nucleic Acids Research (and highlighted as a “Breakthrough Article”) characterizes undesired (and at times, technology-limiting) impurities in that synthesis, providing a mechanistic understanding that will help the design of solutions. The work exploits a modern tool in genomics, RNA-Seq, but applies it in new ways. While gel electrophoresis has been the tool of choice for the past century, this new approach represents a huge advance, identifying not just lengths of RNA, but exact sequences and sequence distributions.
RNA therapeutics companies are already taking notice, particularly those invested in mRNA therapeutics, since chemical synthesis of long RNAs is not a possibility. Impurities in the RNA trigger a potentially lethal immune response, and have been holding back major advances in what could be a key, new therapeutic approach, with wide applicability. This work does not provide the solution, but provides key understandings that may well lead to solutions.
Jianhan Chen recently received a four-year, $600,000 grant from the National Science Foundation to study a newly recognized class of proteins with highly flexible three-dimensional (3D) structural properties, in particular some extra-floppy ones called intrinsically disordered proteins (IDPs).
Proteins are macromolecules that control nearly all aspects of cell function from response to external stimuli to control of cell cycle and cell fate decisions, Chen explains. He adds that IDPs are unusual because while most proteins adopt stable 3D structures to do their work in the cell, IDPs instead remain structurally disordered, that is, extremely flexible. They are believed to account for about one-third of all eukaryotic proteins and are key components of cellular signaling and regulatory networks.
Scientists now believe that by staying flexible, IDPs have an advantage in interacting with other proteins and each other, perhaps because the floppy state lets them respond faster than a more rigid structure, or lets them interact with a wider variety of molecules, or both, Chen says.
Jeanne Hardy, associate professor of chemistry, whose research focuses on a key protein linked to neurological disorders such as Alzheimer’s disease, is being recognized with the inaugural Mahoney Life Sciences Prize at the University of Massachusetts Amherst. A panel of expert judges from the life sciences sector observed that the “biomedical implications are significant” and “this could turn out to be one of ‘the’ pivotal studies in the effort to combat Alzheimer’s.” Hardy will receive the prize and present her research with life sciences experts and UMass officials and scientists at a breakfast ceremony on June 19 at the UMass Club in Boston. “Professor Hardy’s research rose to the top of three highly competitive rounds of review,” said Tricia Serio, dean of the College of Natural Sciences. “Her work exemplifies the outstanding translational research for which our faculty are well known.”
Chemist Vincent Rotello and colleagues at University College London (UCL), U.K., announce that they have developed a “quick and robust” blood test that can detect liver damage before symptoms appear, offering what they hope is a significant advance in early detection of liver disease. Details appear in Advanced Materials.
Their new method can detect liver fibrosis, the first stage of liver scarring that can lead to fatal disease if left unchecked, from a blood sample in 30-45 minutes, the authors note. They point out that liver disease is a leading cause of premature mortality in the United States and U.K., and is rising. It often goes unnoticed until late stages of the disease when the damage is irreversible.
For this work, Rotello and his team at UMass Amherst’s Institute of Applied Life Sciences (IALS) designed a sensor that uses polymers coated with fluorescent dyes that bind to blood proteins based on their chemical processes. The dyes change in brightness and color, offering a different signature or blood protein pattern.
Research institutions still have a long way to go in retaining women in STEM fields, and particularly in the physical sciences, says Sankaran “Thai” Thayumanavan, but this month his chemistry lab celebrated a success as he escorted six women (Celia Homyak, Youngju Bae, Mallory “Molly” Gordon, Priyaa Prasad, and Poornima Rangadurai) receiving their advanced degrees at Graduate Commencement on May 11. He says, “It didn’t dawn on me until we were there at the ceremony, but suddenly I realized ‘Wow!’ We have done something really amazing here. I hooded six women scientists that day, and they have all gone on to find good positions in the physical sciences. That doesn’t happen very often.”
Christie L.C. Ellis, a fourth-year doctoral candidate in chemistry and an advisee of Dhandapani “DV” Venkataraman, whose research focuses on materials used in solar cells, has received a coveted Mass Media Fellowship from the American Association for the Advancement of Science (AAAS). It will send her to work as a science writer at the St. Louis Post-Dispatch for a 10-week internship beginning in June.
Among other benefits, the long-running program will provide Ellis with travel funds, an orientation at AAAS in Washington, D.C., a stipend and training in interviewing skills and news judgment. She expects to shadow a science writer at the newspaper for a short time and then work on her own stories. “I feel really fortunate to have this fellowship. They’re giving me a really great opportunity and investing a lot in me,” she says.
Her advisor says, “Christie is passionate about communicating science to a broad audience. Therefore, this prestigious fellowship will provide a fantastic opportunity for her to learn from experts in the media industry and closely interact with them. We are eager to learn from Christie’s experience and improve our science communication skills.”
Professor Paul Dubin passed away May 22, 2018.
His research interest was polyelectrolytes and long-chain molecules in which every repeat unit carries a charge, with focus on their interaction with oppositely charged molecules such as surfactant micelles, nanoparticles and proteins, with the objective of fundamental understanding of solution behavior.
In an unexpected finding, chemist Sankaran “Thai” Thayumanavan and colleagues at the University of Massachusetts Amherst show for the first time how movement of a single chemical bond can compromise a membrane made up of more than 500 chemical bonds. Their system uses light as a switch to create a reversible, on-demand molecular control mechanism.
Thayumanavan explains, “There are many applications that one can imagine developing from these fundamental findings, especially ones that need controlled release. For example, we have shown that two compounds that would readily react with each other can be in the same solution but are separated by a very thin membrane made of a few nanometers and therefore do not react with each other.”
“But upon exposure to light, the membrane gets compromised to allow the two components to react with each other,” he adds. “The interesting thing is that the membrane is not permanently compromised upon exposure to light, but only when the light is on.”
His postdoctoral associate Mijanur Rahaman Molla and doctoral student Poornima Rangadurai conducted most of the experimental work. The UMass Amherst group also collaborated with theoretical chemists Lucas Antony and Juan de Pablo at the University of Chicago, who modeled the system in order to more deeply understand it, Thayumanavan notes. Details are online now in Nature Chemistry.