Mahoney Life Sciences Prize

Stefan K. Baier ’03 PhD

Principal Consultant, PlaFooTex Consulting, LLC
University of Bonn | Dipl.-Ing, Food Engineering, 1999
University of Massachusetts Amherst | PhD, Food Science, 2003

Stefan Baier is an expert food material scientist and technical leadership executive, currently the principal consultant at PlaFooTex Consulting LLC, where he advises on technical strategy, R&D capabilities, and delivers scientific insights to enable product innovation for companies within the alternative protein, fermentation, and broader food technology sectors. Stefan also serves as an Adjunct Associate Professor with the University of Queensland’s School of Chemical Engineering in Brisbane, Australia, and is on the editorial board of the Journal of Texture Studies. With over 23 years of food industry experience, Stefan has a uniquely comprehensive perspective, having worked across the full spectrum from B2B to B2C, ingredients and processing to finished products, and from startups to major corporations. His career spans leadership roles at organizations like Aqua Cultured Foods, Inc., Bühler Group AG, Motif FoodWorks, PepsiCo, Frito-Lay NA, and Cargill, providing him with insight into both private and public sectors, and the ability to navigate diverse operational scales and business models. He has contributed to a portfolio of 10+ patents, authored 35+ peer-reviewed publications, and secured over $10 million in research grants. Stefan earned a PhD in Food Science from the University of Massachusetts Amherst and an Engineering degree (Dipl.-Ing) in Food Technology & Engineering from Rheinische Friedrich-Wilhelms Universität in Bonn, Germany.

Richard J. Gregory ’86 PhD

Fellow, American Institute for Medical and Biological Engineering
University of Massachusetts Amherst | PhD, Biochemistry, 1986

Richard Gregory received his PhD in Biochemistry from the University of Massachusetts Amherst, 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.

Dennis Guberski ’75, ’83 MS

Founder, Biomere & Mucosal Vaccine Technologies LLC
University of Massachusetts Amherst | BS and MS, Animal Science, 1975 and 1983

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. Following the sale of Biomere he served as the managing partner for Mucosal Vaccine Technologies, a vaccine company that was working on a therapy for Genintal Herpes HSV-2.

David J. Mazzo ’81 MS, ’84 PhD

President and Chief Executive Officer, Lisata Therapeutics
Villanova University | BS, Chemistry, and BA, Interdisciplinary Humanities, 1979
University of Massachusetts Amherst | MS and PhD, Chemistry, 1981 and 1984

David J. Mazzo is the President and CEO of Lisata Therapeutics, Inc., a clinical stage therapeutics development biopharmaceutical company dedicated to the discovery, development, and commercialization of innovative therapies for the treatment of advanced solid tumors and other major diseases. Lisata’s internalizing RGD, or arginylglycylaspartic acid, (iRGD) cyclic peptide product candidate, certepetide, is an investigational drug designed to initiate the C-end rule active transport pathway that allows co-administered or tethered anti-cancer drugs to selectively target and penetrate solid tumors more effectively. Certepetide has also been shown to make the tumor microenvironment less immunosuppressive, to recruit cytotoxic T cells to the tumor and to inhibit the metastatic cascade. Dr. 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 40 years of successful global product development, registration, and launch. Dr. 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.

Vic Myer

Scientific Advisor
Cornell University | BS, Biochemistry & Molecular Biology, 1989
Yale University | PhD, Biochemistry & Molecular Biology, 1995

Vic Myer, PhD is a seasoned scientific leader with more than 25 years of research and development experience.  A former CSO and CTO, he currently advises by sitting on two Boards of Directors, four Scientific Advisory Boards, is an advisor to the NIH SCGE, and is an advisor to Atlas Venture.  His most recent role was President and Chief Scientific Officer at Chroma Medicine where he helped build that epigenetic editing company from idea to successful proof of concept in NHPs with a clear path to the clinic. Previously, he was Chief Technology Officer of Editas Medicine where he led the genome-editing platform, CMC, and chemistry departments.  At the Novartis Institutes for Biomedical Research, he led a large, technology focused target discovery, target validation and lead finding group in the Developmental and Molecular Pathways department for 11 years. Prior to Novartis, Vic focused on industrializing and using ‘omics technologies at Millennium, Akceli and Corning. He has B.S. from Cornell, a PhD from Yale and did his post-doc at MIT/The Whitehead Institute.

Charles H. Sherwood ’72 MS, ’77 PhD

Founder and Former CEO, Anika Therapeutics
Cornell University | BS, Chemical Engineering, 1970
University of Massachusetts Amherst | MS and PhD, Polymer Science, 1972 and 1977

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

Adjunct Professor, Chemistry Dept, Holyoke Community College
University of Massachusetts Amherst | BS, MS, and PhD, Chemistry, 1972-1980

Diane Stengle got her BS, MS, and PhD from UMass Amherst. In her PhD research, she specialized 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. She worked for Monsanto Co. as a research scientist in polyacrylate solutions for pressure-sensitive adhesives and coatings. Since 1994, she has been a chemistry faculty at Holyoke Community College in Massachusetts.

Monica Tan ‘98

Senior Vice President of Product & Design, Science Exchange
University of Massachusetts Amherst | BS, Biology, 1998

Monica Tan is the Senior Vice President of Product and Design at Science Exchange, headquartered in Palo Alto, California. A seasoned expert in creating transformative software experiences, Monica previously served as Director of User Experience Design at cybersecurity firms Anomali and AlienVault (acquired by AT&T in 2018), where she leveraged insights into human psychology and behavior to optimize digital user journeys. She has also collaborated with leading companies such as Intuit, Cisco, Citrix, and Apple. At Science Exchange, she drives end-to-end product development, aligning strategy with market needs to deliver impactful solutions, culminating in an acquisition by Waud Capital Partners. She holds a Bachelor’s degree in Biology with a minor in Psychology from the University of Massachusetts, Amherst.

Carrie Williams ‘02

University of Massachusetts Amherst | BS, Biology, 2002
University of California at Berkeley | MBA, 2009

Carrie brings over 20 years of healthcare experience from several vantage points within the industry. She started her career in biopharma, managing clinical trials for oncology drugs. She then spent time in McKesson’s strategy and business development group before joining Omada Health, where she served as Vice President, Strategy and Business Development and focused heavily on all elements of commercial strategy. She then rejoined McKesson where her investment focus is on digital health, including early stage tech-enabled healthcare services and software companies. Williams earned her MBA from the Haas School of Business at the University of California at Berkeley and has a BS in biology from the University of Massachusetts Amherst. 

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.

Lynne A. McLandsborough, PhD

Distinguished Professor of Food Microbiology and Interim Director of the Center for Agriculture, Food, and the Environment, UMass Amherst 
2024 Recipient

The industry panel awarded the 2024 Mahoney Life Sciences Prize to Lynne McLandsborough, professor of food microbiology and interim director of the Center for Agriculture, Food, and the Environment (CAFE) at UMass Amherst. Her research aims to devise a more effective and efficient cleaning and sanitation method for companies that process low-moisture foods like peanut butter and chocolate. “Outbreaks of salmonellosis associated with low-moisture foods are a persistent problem,” says McLandsborough. The facilities that process these products use a dry cleaning method to clean equipment, which removes residues but doesn’t kill bacteria like salmonella. McLandsborough and her team created an acidified water-in-oil emulsion that significantly increases antimicrobial activity. Using this method, processors can enhance bacteria eradication and sanitize processing lines without waiting for equipment to cool down. Since publication of these findings, McLandsborough has presented this research to M&M Mars and talked with chocolate supplier Barry Callebaut about testing this technology in a chocolate pilot plant.

Learn more about Lynne A. McLandsborough, PhD.

Lynn Adler

Professor, Biology Department
2022 Recipient

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
2021 Recipient

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
2020 Recipient

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
2019 Recipient

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.

Jeanne Hardy

Associate Professor, Department of Chemistry
2018 Recipient

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.