Mahoney Life Sciences Prize
The Mahoney Life Sciences Prize is awarded annually to honor excellence and recognize academic achievement that propels significant advances in science and industry. One award will be made to a faculty member whose primary appointment is within the UMass Amherst College of Natural Sciences and who was the principal author of a peer-reviewed paper reporting original research performed at UMass and published during the previous three years.
Review of applications and award of the Mahoney Life Science Prize focuses on the quality of the published paper, the potential for the research findings to address a major scientific challenge, and an assessment of the potential translatable and practical applications of the research findings to industry. The paper can be on any topic in the life sciences that is new research with translatable applications to industry and society.
The prize includes a cash award of $25,000 to the winning applicant as well as opportunities to present the research to industry leaders and the UMass Amherst community.
The CNS Mahoney Life Science Prize is currently open for applications for the 2023-24 cycle until October 24, 2023.
Eligibility and Application Process
- Eligibility is limited to faculty members whose primary appointment is in the College of Natural Sciences.
- The applicant must be the primary author of the submitted paper, regardless of the number of co-authors.
- The submitted paper must have been published in a peer-reviewed scientific journal with a publication date later than October 24, 2020. Accepted papers that have not yet been published are ineligible.
- CNS faculty members may re-apply in successive years, with the exception of previous Mahoney Life Science Prize winners.
How to Apply
Go to the InfoReady online Internal Opportunities system, click on the CNS Mahoney Prize listed among the Open Competitions, read the instructions, and finally click the "Apply" button to start your online application. Complete the requested contact information. Attach three separate documents in PDF or Microsoft Word format:
- ESSAY - Describe how this research paper has made a substantial contribution to the field since its publication, as well as the potential for these findings to continue to significantly inform and affect a major scientific challenge. If applicable, essay submissions should provide a discussion of the translatable and practical applications of the research to industry. Maximum length: 500 words.
- PAPER - Attach a PDF of the published paper.
- CV - Attach your curriculum vitae.
Reviewers from both academia and industry will read and score the applications, with the objective of identifying a pioneering scientist whose paper in any subfield of the life sciences provides a groundbreaking study with findings that hold great promise for the field. There are two stages of review:
- Stage 1 Review: A representative group of eminent researchers within the UMass Amherst College of Natural Sciences, screened for conflicts of interest, will review all applications and select the top 10 papers for consideration at the next level.
- Stage 2 Review: A select external advisory committee of industry leaders and alumni scholars in the field will review the top 10 papers and choose one paper to recommend for award of the 2023-24 CNS Mahoney Life Sciences Prize.
Applicants will be notified of the outcome of the Stage 1 Review stage in December 2023. The outcome of the final selection process will be communicated to finalist applicants in early spring, followed by a public announcement of the prize.
For questions about any aspect of this application process, please contact Michael Wright, CNS Director of Research Development, at michael [dot] wright [at] umass [dot] edu (michael[dot]wright[at]umass[dot]edu).
2022 Industry Judges
Stefan K. Baier
Head of Food Science and Technology, North America Buhler Inc.
Stefan K. Baier is the Head of Food Science and Technology at North America Buhler Inc. and an Adjunct Associate Professor with the School of Chemical Engineering at the University of Queensland in Brisbane, Australia. Baier received a degree in Food Engineering (Dipl.-Ing.) from the Rheinische Friedrich-Wilhelms Universität in Bonn, Germany, and a PhD in Food Colloids and Biopolymers from the University of Massachusetts Amherst, under Professor Julian McClements. Prior to joining Motif FoodWorks, Dr. Baier served as an Associate Fellow with PepsiCo and was a Senior Scientist at Global Food Research with Cargill, Inc. Dr. Baier’s research interests are in the area of food oral processing with an emphasis on rheology and tribology. He and his research team leverage soft matter and colloidal physics coupled with engineering principles to develop rational design criteria for the next generation low-fat, sodium and sugar foods and beverages based on insights from food oral processing. Dr. Baier sits on the editorial board for the Journal of Texture Studies and BioTribology. He is a Fellow at the Royal Society of Chemistry. He initiated PepsiCo’s participation in the EIT-Food, a major EU initiative for innovation in the food industry and has several industrial grants across the globe, including an ARC Linkage and AiF grant to develop food oral processing as a scientific discipline. Dr. Baier is the recipient of the 2015 Uniquest Partners in Research Excellence Awards. He has several key impact publications and has given several keynote presentations on the role of rheology and tribology in oral processing, e.g., more recently at Neutrons & Foods, International Conference on BioTribology (ICoBT) and the FDA/PQRI conference.
Leslie Dierauf, ’70 BS
Director, Retired, U.S. Geological Survey’s Pacific Northwest
Leslie Dierauf was the first woman to apply to, and get accepted into, veterinary school (University of PA) from the University of Massachusetts back in 1969. She is a 1970 graduate of UMass Amherst (Microbiology and English), and a retired wildlife veterinarian and conservation biologist, who worked with the federal government for more than 20 years. Prior to retiring in 2011, Dierauf was the U.S. Geological Survey’s Pacific Northwest director, overseeing science research related to natural hazards, climate variability, water quality and quantity, geologic and geographic mapping, and biological resources in Washington, Oregon, and Idaho. From 2004 to 2008, Dierauf served as director of the National Wildlife Health Center (NWHC) in Madison, Wisconsin. Before that, she worked with the U.S. Fish and Wildlife Service on its Endangered Species program for the Southwest. Dierauf also was a science advisor on Committee staff for the U.S. House of Representatives in Washington, D.C., for over three years. In late 1998, she received the American Veterinary Medical Association’s National Animal Welfare Award. She also was a Congressional Science Fellow (American Association for the Advancement of Science) in 1990, and President of the International Association for Aquatic Animal Medicine in 1987. In 2018, Dierauf published a third edition of The CRC Handbook of Marine Mammal Medicine. Currently, Dierauf supports the SeaDoc Society as well as SeaLife Response, Rehabilitation and Research (SR3). She is a big supporter and follower of OneHealth initiatives around the world, too.
Richard J. Gregory, ’86 PhD
Fellow, American Institute for Medical and Biological Engineering
Richard Gregory received his PhD in Biochemistry from the University of Massachusetts Amherst in 1986, followed by post-doctoral research in cancer genetics at the Worcester Foundation for Experimental Biology in Shrewsbury, Mass. In 1989, he joined Genzyme Corporation, where he was responsible for discovery projects in the molecular biology department. In 1990, his group at Genzyme was the first to express the cystic fibrosis transmembrane conductance regulator (CFTR) protein and to determine the molecular defect caused by the most common mutation of CFTR. From 1993 to 1995 he was Director of Molecular Biology at Canji, Inc. in San Diego, where he led research and development of therapeutics based upon tumor suppressor genes. Gregory returned to Genzyme in 1995 as Vice President for Gene Therapy. Efforts under his direction during this period included programs in cancer immunotherapy, gene therapies for genetic diseases, and cardiovascular gene therapy. In 2001, Gregory became Senior Vice President and Head of Research for Genzyme Corporation where he was responsible for early R&D, from discovery to development, in all therapeutic areas at Genzyme. In 2011, he was appointed Head of the Sanofi Genzyme R&D Center, overseeing R&D in rare diseases, multiple sclerosis, immune disorders, and tissue protection/regenerative medicine. In January of 2015, Gregory joined ImmunoGen, where he was responsible for research leading to new antibody-based therapeutics to address the unmet needs of patients with cancer. Since September of 2019 Gregoryd has been an independent consultant. He is the co-author of over 60 peer-reviewed publications and 23 issued U.S. patents in the area of biotechnology. Gregory is a Fellow of the American Institute for Medical and Biological Engineering.
Founder, Biomere & Mucosal Vaccine Technologies LLC
Mr. Dennis Guberski, a geneticist trained at the University of Massachusetts Amherst, spent more than 20 years (1977-1997) at the University of Massachusetts Medical Center both as a researcher and an administrator in the Department of Pathology. During this time, he extensively studied the etiology of Type 1 diabetes and developed several spontaneous animal models that are still in widespread use today. He was the first to report on the perturbation of autoimmune disease by a parvovirus, which caused disease impacting both the pancreas and thyroid. In 1996, he founded Biomere, a preclinical contract research organization that employed 125 FTEs when sold to Joinn Ltd. in December 2019. At Biomere, Mr. Guberski served as PI on numerous NIH grants and contracts, including the $4.9MM Type 1 diabetes Preclinical Testing Program in support of the government's Trial Net. His longstanding contribution to science includes key papers elucidating the pathogenesis of Type 1 diabetes, mapping susceptibility genes for Type 1 diabetes/rheumatoid arthritis, and developing novel models for environmental initiation of autoimmunity. He is currently the managing partner for Mucosal Vaccine Technologies LLC, a vaccine company working on a therapy for Genital Herpes HSV-2 that should be in clinical trials in Q4 2021.
David J. Mazzo, PhD, MS
President and Chief Executive Officer, Caladrius Biosciences
David J. Mazzo is the President and CEO of Caladrius Biosciences, Inc., a late-stage therapeutics development biopharmaceutical company pioneering advancements of cell therapies for select cardiovascular and autoimmune diseases. The company’s primary technology platform is based on the use of CD34+/CXCR4+ cells for ischemic repair in a variety of indications, including critical limb ischemia, coronary microvascular disfunction, and no-option refractory disabling angina (NORDA). Mazzo is a pharmaceutical executive and strategic leader with broad experience in both large and small companies gained from working in a variety of multicultural and multilingual environments in the USA, Canada, Europe, and Asia. He is recognized for his exceptional strategic, scientific and regulatory expertise, upon which he has amassed a track record of more than 35 years of successful global product development, registration, and launch. Mazzo earned his PhD in Analytical Chemistry as well as an MS in Chemistry at the University of Massachusetts Amherst. He also holds dual degrees [BS in Chemistry and BA in Honors (Interdisciplinary Humanities)] from Villanova University. He complemented his American education with a Research Fellowship at the Ecole Polytechnique Fédérale de Lausanne in Switzerland.
Entrepreneur in Residence, Atlas Venture
Vic Myer is president and CSO of Chroma Medicine. Previous to that he was the Chief Technology Officer at Editas Medicine and was responsible for delivering enabling technologies to bring genomic medicines to the clinic. Myer served as executive director and Cambridge site head for the developmental and molecular pathways department at the Novartis Institutes for Biomedical Research Incorporated (NIBR), where he also served as a research investigator, led the high-throughput biology team, and oversaw the target discovery technologies platform. He was also a founding scientist and group leader at Akceli, Inc., a venture-backed systems-biology company, served as senior scientist for Millennium Pharmaceuticals, and held various roles at Corning, Inc. Myer received his BS in biology and biochemistry from Cornell University and his PhD in molecular biophysics and biochemistry from Yale University.
Chuck Sherwood, ’72 MS, ’77 PhD
Founder and Former CEO, Anika Therapeutics
Charles H. Sherwood was the Chief Executive Officer of Anika Therapeutics from 2002 to 2018. From 2002 through July 2017, he also held the title of President. Sherwood joined Anika in 1998 with extensive experience in research, engineering, manufacturing, quality assurance, regulatory affairs, and business management. He first served at Anika in the position of Vice President of Research, Development, and Engineering. Prior to joining Anika, he was a senior director with Chiron Vision, responsible for medical product development and commercialization. From 1982 to 1995, Dr. Sherwood was with IOLAB Corporation, a division of Johnson & Johnson, where he led the Research and Product Development organization. Earlier, he held various technical and management positions with Hughes Aircraft Company and Lord Corporation. He was also on the faculty of California State Polytechnic University, Pomona. Sherwood holds a BS in chemical engineering from Cornell University, an MS and a PhD in polymer science and engineering from the University of Massachusetts Amherst, and a certificate in management from Claremont Graduate School.
Diane Stengle, ’80 PhD
Associate Professor, Chemistry Dept, Holyoke Community College
Diane Stengle got her BS, MS, and PhD from UMass Amherst. She specialize in solid state 1H NMR applied to the orientation of polymer molecules in strained systems, including theoretical models of simple carbon chains such as polyethylene. Previously, she worked for Monsanto Co. as a research scientist in polyacrylate solutions for pressure-sensitive adhesives and coatings. Since 1994, she has been a professor of chemistry at Holyoke Community College in Massachusetts.
Vice President of Product, Science Exchange
Monica Tan, VP of Product, Science Exchange (based in Palo Alto, Calif.) is a seasoned driver of transformative software user experience. As Director of User Experience Design at cybersecurity firms Anomali and AlienVault (acquired by AT&T in 2017), she analyzed human psychology and behavior and used her findings to optimize users’ digital journeys. In addition, she has worked and consulted with Intuit, Cisco, Citrix, Apple, and others. Currently, Monica applies her expertise to Science Exchange’s technology platform for life sciences R&D, helping researchers at major biopharma and biotechnology companies accelerate breakthrough discoveries. At UMass Amherst, Monica was trained in Biology (BS) and Psychology (minor).
Mahoney Life Sciences Prize: History
The Mahoney brothers all received their degrees in Chemistry from the University of Massachusetts Amherst. They went on to become leaders in their own industries and have served as high-level alumni advisers to the campus. The Mahoney brothers encourage the university to think differently about the way it serves its students and promotes the UMass Amherst education. Their commitment to student success is seen in their extraordinary efforts to personally mentor students and train other alumni to do the same, while their family legacy of giving and involvement is seen far and wide throughout the campus. The Mahoney Life Sciences Prize, like all that this family does for its alma mater, seeks to inspire and recognize greatness.
Past Mahoney Prize Recipients
Professor, Biology Department
Adler, L. S., Barber, N. A., Biller, O. M., & Irwin, R. E. (2020). Flowering plant composition shapes pathogen infection intensity and reproduction in bumble bee colonies. In Proceedings of the National Academy of Sciences (Vol. 117, Issue 21, pp. 11559–11565). Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.2000074117
Pathogens pose significant threats to pollinator health and food security. Pollinators can transmit diseases during foraging, but the consequences of plant species composition for infection is unknown. In agroecosystems, flowering strips or hedgerows are often used to augment pollinator habitat. We used canola as a focal crop in tents, and manipulated flowering strip composition using plant species we had previously shown to result in higher or lower bee infection in short-term trials. We also manipulated initial colony infection to assess impacts on foraging behavior. Flowering strips using high-infection plant species nearly doubled bumble bee colony infection intensity compared to low-infection plant species, with intermediate infection in canola-only tents. Both infection treatment and flowering strips reduced visits to canola, but we saw no evidence that infection treatment shifted foraging preferences. Although high-infection flowering strips increased colony infection intensity, colony reproduction was improved with any flowering strips compared to canola alone. The effects of flowering strips on colony reproduction were explained by nectar availability, but the effects of flowering strips on infection intensity were not. Thus, flowering strips benefited colony reproduction by adding floral resources, but certain plant species also come with a risk of increased pathogen infection intensity.
Read more about Lynn Adler.
Margaret A. Riley
Professor, Biology Department
Roy, S.M. and Riley, M.A. (2019). Evaluation of the Potential of Colicins to Prevent Extraluminal Contamination of Urinary Catheters by Escherichia Coli. International Journal of Antimicrobial Agents, (54)5, 619-625. https://www.sciencedirect.com/science/article/abs/pii/S0924857919301840?...
The feasibility of using colicins to create an antimicrobial lubricant to prevent extraluminal catheter contamination during urinary catheter insertion was assessed. Levels of resistance of uropathogenic Escherichia coli to antibiotics and colicins were compared. The results showed that antibiotics and colicins possess similar frequencies of resistance to a single drug, whereas colicins exhibit significantly lower levels of multidrug resistance (22%) than antibiotics (42%). Colicins and antibiotics showed complementary inhibitory activity, with each targeting different subsets of pathogenic isolates. The collateral impact of these two antimicrobials on genera that are members of the fecal/vaginal/urinary microbiome was assessed, with colicins showing significantly less collateral damage than antibiotics. Using a novel colicin, SR4, minimum inhibitory concentrations (MICs) for a panel of 30 uropathogenic isolates were determined and showed that SR4 achieved the same antimicrobial efficacy as gentamicin using 20-30% less drug. An SR4-impregnated catheter lubricant was created and its ability to prevent extraluminal urinary catheter contamination in vitro was demonstrated. These data indicate that a colicin-impregnated lubricant may provide a viable prophylactic option for preventing catheter-associated urinary tract infections.
Read more about Margaret A. Riley.
Dr. Derek R. Lovley
Distinguished Professor, Department of Microbiology
Ueki, T., Walker, D. J. F., Tremblay, P.-L., Nevin, K. P., Ward, J. E., Woodard, T. L., Nonnenmann, S. S., & Lovley, D. R. (2019). Decorating the Outer Surface of Microbially Produced Protein Nanowires with Peptides. ACS Synthetic Biology, 8(8), 1809–1817. https://doi.org/10.1021/acssynbio.9b00131
The potential applications of electrically conductive protein nanowires (e-PNs) harvested from Geobacter sulf urreducens might be greatly expanded if the outer surface of the wires could be modified to confer novel sensing capabilities or to enhance binding to other materials. We developed a simple strategy for functionalizing e-PNs with surface-exposed peptides. The G. sulf urreducens gene for the monomer that assembles into e-PNs was modified to add peptide tags at the carboxyl terminus of the monomer. Strains of G. sulf urreducens were constructed that fabricated synthetic e-PNs with a six-histidine “His-tag” or both the His-tag and a nine-peptide “HA-tag” exposed on the outer surface. Addition of the peptide tags did not diminish e-PN conductivity. The abundance of HA-tag in e-PNs was controlled by placing expression of the gene for the synthetic monomer with the HA-tag under transcriptional regulation. These studies suggest broad possibilities for tailoring e-PN properties for diverse applications.
Read more about Dr. Derek R. Lovley.
S. "Thai" Thayumanavan
Professor, Department of Chemistry
Dutta, K., Hu, D., Zhao, B., Ribbe, A. E., Zhuang, J., & Thayumanavan, S. (2017). Templated Self-Assembly of a Covalent Polymer Network for Intracellular Protein Delivery and Traceless Release. Journal of the American Chemical Society, 139(16), 5676–5679. https://doi.org/10.1021/jacs.7b01214
Protein-based drugs have great potential for improving our ability to treat disease. In comparison to current drugs that are based on small molecules, drugs composed of proteins are more effective for addressing specific genetic deficiencies without undesirable side effects. However, there are major challenges in delivering proteins into and within a cell. These challenges are related to keeping the protein stable, avoiding unwanted immune system response, and translocating the protein across the cellular membrane.
This study presents a novel and practical strategy which simultaneously overcomes all of these challenges. In this strategy, the polymers self-assemble to form a sheath around the protein, analogous to "shrink-wrapping" the protein. The polymer sheath encapsulates proteins, preserves their structure and function during delivery, and releases them when the assembly enters the cell cytosol. The polymers do not provoke an unwanted immune system response, and do not leaving any residue behind. This strategy is applicable to a broad range of proteins, and the sheath can be designed to release its cargo under various conditions. In addition to the applications for protein therapeutics and devices, the technology can be used to design reagents for basic biochemical research. Dr. Thayumanavan is currently working with industry partners toward both applications, in part through his start-up company, Cyta Therapeutics.
Read more about S. "Thai" Thayumanavan.
Associate Professor, Department of Chemistry
Dagbay, K. B., & Hardy, J. A. (2017). Multiple proteolytic events in caspase-6 self-activation impact conformations of discrete structural regions. Proceedings of the National Academy of Sciences, 114(38), E7977–E7986. https://doi.org/10.1073/pnas.1704640114
The challenges wrought by Alzheimer's disease are increasing with the graying of society in the developed world. In the United States, Alzheimer's disease promises to be the single largest medical expense ($1.1 trillion annually) by 2050. Today, no suitable treatments for Alzheimer's disease exist. Associate Professor in Chemistry Jeanne Hardy has been working for more than a decade to understand an important protein involved in Alzheimer's disease, called caspase-6. Recently, Dr. Hardy made important discoveries that may significantly advance our ability to treat this increasingly relevant disease.
People with Alzheimer's disease have tangles associated with the neurons of their brains. There is evidence that the caspase-6 protein is responsible for creating those tangles. Inhibiting caspase-6 could be one of the most promising approaches for treating Alzheimer's disease. In order to do this with a positive outcome, it is important not to inhibit any of the other 11 caspases. This is a major challenge, because all of the caspase proteins perform very similar reactions.
Dr. Hardy has risen to this challenge. In 2011, the Hardy lab found that one part of caspase-6 can fold into a helix, which no other caspase can do. However, caspase-6 does not maintain a helix shape all of the time, but constantly fluctuates between a helix and a three-strand shape. Last year, the Hardy lab used a state-of-the-art method to take snapshots of what parts of caspase-6 change shape and fluctuate over time. Insights from this study have allowed the Hardy Lab to develop new chemicals, targeting caspase-6 without affecting other caspases. This development represents a pivotal step forward toward treating Alzheimer's disease with caspase-6 inhibitors.