Past Seminars & Events

Professor Bobby Arora
Department of Chemistry
NYU

Short stories in molecular recognition (of protein surfaces) and catalysis (of amide bonds)

Protein-protein complexes are difficult targets for inhibitor design, and therefore, offer a testing ground for new approaches. We are developing a rational design approach that begins by mimicry of protein interfaces by constrained peptides and peptidomimetics. The first part of this presentation will discuss the application of our approach to the discovery of inhibitors for oncogenic targets Ras and, the intrinsically disordered, Myc. The second part of the talk will focus on a rational design approach to develop catalysts for peptide bond formation. This work aims to address the significant challenge of excess reagent use in peptide synthesis.

Paramjit Arora

Paramjit Arora is a Professor of Chemistry at New York University. He obtained his B.S. and Ph.D. in Chemistry from UC Berkeley and UC Irvine, respectively. He was an American Cancer Society postdoctoral fellow at the California Institute of Technology before joining the faculty of New York University. His research focuses on designer protein mimics that modulate biomolecular interactions.

Hosted by Professor William Pomerantz

Professor Richard Vachet
Department of Chemistry
University of Massachusetts Amherst

Protein Structure, Binding, and Aggregation in Complex Mixtures

Characterizing the higher-order structures (HOS) and interactions of proteins in complex mixtures is challenging and requires the development of new tools. Mass spectrometry (MS)-based techniques are emerging as valuable tools in structural biology, and among these tools covalent labeling (CL) methods have some unique advantages that can be exploited to study protein structure, protein interactions, and protein aggregation, including in live cells. In CL-MS, HOS and binding information are encoded via the formation of covalent bonds that can survive the many steps (i.e. cell lysis, extraction, digestion, separation, MS/MS) needed to analyze proteins by MS. We are developing and applying new CL-MS methods to study the pre-amyloid forms of two important amyloid systems. One is β-2-microglobulin (β2m), which forms amyloids in dialysis-related amyloidosis. The second is Tau, which is important in various tauopathies such as Alzheimer’s disease. We are also developing an approach that can study Tau binding to the low-density lipoprotein receptor-related protein 1 (LRP1) in live cells. In our work on β2m, we have used CL-MS to characterize the initial amyloidogenic change that this protein undergoes and have mapped the energy landscape of this structural change. In addition, we have used CL-MS to determine the structures of pre-amyloid oligomers that have led to the development of small- molecule inhibitors that prevent β2m amyloid formation. Our work on Tau is focused on understanding the transition of this structurally disordered protein into ordered aggregates, and we have also recently been studying its interaction with LRP1, which is a membrane-associated receptor that is a critical determinant for Tau spread and aggregation. To study the ordering of Tau’s structure as it aggregates, we use native MS to monitor its conformational heterogeneity over time. Tau binding to LRP1 relies on CL-MS based mapping of this protein-receptor interaction on live H4i neuroglioma cells. Tau-LRP1 interactions promise to reveal potential approaches for drug intervention for Tau uptake.

Richard Vachet

Richard Vachet is a Professor in the Chemistry Department at the University of Massachusetts Amherst. He received a Ph.D. in Analytical Chemistry from the University of North Carolina- Chapel Hill and did postdoctoral research at the US Naval Research Laboratory from 1997 to 1999 as a National Research Council Postdoctoral Research Associate. He began his independent career at the University of Massachusetts Amherst in 1999. His current research focuses on (a) the development and application of mass spectrometry-based methods to study protein amyloid formation; (b) the development of new tools to study the higher order structure of protein therapeutics; and (c) the detection and imaging of nanomaterial drug delivery agents in biological systems. He has published over 180 peer-reviewed journal articles and has been a member of the Editorial Board of the Journal of the American Society for Mass Spectrometry and the Features Panel for Analytical Chemistry. He has also won several awards, including the Outstanding Research Award from the University of Massachusetts Amherst, the GlaxoSmithKline Lectureship in Analytical Chemistry, and the Young Investigator Award from the American Society for Mass Spectrometry.

Hosted by Professor Varun Gadkari

Professor Tara Meyer
Department of Chemistry
University of Pittsburgh

The Effects of Sequence and Architecture on the Degradation of Polyesters

Renewable biodegradable polymers such as poly(lactic- co-glycolic acid) (PLGA) are widely used in materials and biomedical contexts, yet their degradation behavior is typically controlled through coarse variables such as overall composition or molecular weight. The Meyer group has found that molecular-level structure, specifically monomer sequence and macromolecular architecture, provides a more precise and predictive handle on degradation in PLGA-based materials. Dramatic differences in hydrolytic degradation are observed for polymers with identical composition but subtly different monomer order, revealing a strong sensitivity to local connectivity. Related effects emerge in PLGA brush architectures, where sequence combines with grafting density and backbone-side chain organization to further regulate water access and bond cleavage.

Tara Meyer

Tara Y. Meyer received her B.A. from Grinnell College in 1991 and her Ph.D. from the University of Iowa in 1991 (Advisor Louis Messerle). She carried out postdoctoral work at both the University of Iowa (1991-2) under the supervision of Prof. Richard F. Jordan and at the University of California, Berkeley (1992-4) under the joint supervision of Prof. Robert G. Bergman and Bruce M. Novak. Dr. Meyer joined the faculty at the University of Pittsburgh Department of Chemistry in 1994 and has served the University in a variety of roles including as Asst. Dean for Graduate Studies and Senior Advisor to the Dean. Her research has been recognized by both CAREER and Sloan Foundation Awards and a sabbatical stay at MIT (2003) was supported by an NIH Ruth L. Kirschstein National Research Service Award. Dr. Meyer co-edited the first ACS symposium series on sequence-controlled polymers and was a co-organizer of symposia on the topic at 2013 & 2016 ACS Meetings and 2015 Pacifichem meeting.

Hosted by Professor Lamb

Professor Laura Kiessling
Department of Chemistry
Massachusetts Institute of Technology

Multivalent Probes of Protein-Glycan Interactions

Glycan-binding proteins coordinate essential biological functions through multivalent recognition, but the basic principles behind these interactions are not fully understood. This presentation explores how synthetic polymers can serve as tunable platforms for decoding and recapitulating multivalent protein- glycan interactions. By systematically varying glycan density, spacing, and presentation on polymer scaffolds, we dissect the mechanistic underpinnings of avidity and specific biological recognition. We have leveraged these insights to design polymeric systems that mimic key features of mucins, the proteins that constitute our protective mucus. These synthetic glycopolymers also serve as multivalent signaling agents, engaging multiple receptors at once to enhance cellular responses with high specificity. This seminar will highlight how chemical synthesis and polymers can be used to investigate and harness nature’s multivalent recognition strategies.

Laura Kiessling

Laura Kiessling earned a BS in Chemistry from the Massachusetts Institute of Technology and a Ph.D. in Organic Chemistry from Yale University. After two years at the California Institute of Technology as an American Cancer Society Postdoctoral Fellow, she joined the faculty of the University of Wisconsin, Madison in 1991. In 2017, she returned to MIT as the Novartis Professor of Chemistry and Member of the Broad Institute. She is also a Member of the Koch Institute and an Associate Member of the Ragon Institute. Her interdisciplinary research interests have advanced our understanding of cell surface recognition processes, especially those involving protein-glycan interactions. Laura is a Fellow of the American Association for the Advancement of Science, and a Member of the American Academy of Microbiology, the National Academy of Sciences, and the National Academy of Medicine. She was the founding Editor–In-Chief of ACS Chemical Biology. Her honors and awards include a MacArthur Foundation Fellowship, a Guggenheim Fellowship, the ACS Gibbs Medal, the Tetrahedron Prize, the Centenary Prize of the Royal Society of Chemistry, and the Ronald Breslow Award for Achievement in Biomimetic Chemistry.

Hosted by Professor Erin Carlson and Professor Theresa Reineke

Professor Laura Kiessling
Department of Chemistry
Massachusetts Institute of Technology

Chemical Probes of Bacterial Glycans

Bacteria rely on their microbial glycans to survive. Moreover, they use this glycan covering to mediate host colonization, pathogenesis, and regulate immune responses. Controlling the microbes that live in us – to our benefit or detriment – requires new strategies to detect and visualize their glycans. Our group has developed novel chemical probes image and report on microbial polysaccharides. This talk will describe new methods that rely on new chemistry to visualize critical glycans within the carbohydrate coat of Mycobacterium tuberculosis and related pathogens. Using these chemical probes, we have uncovered a vulnerability in the cell envelope that can be exploited to enlist host clearance. An increased understanding of the pathways and functions of these non-human glycans will aid in combating and controlling infectious diseases.

Laura Kiessling

Laura Kiessling earned a BS in Chemistry from the Massachusetts Institute of Technology and a Ph.D. in Organic Chemistry from Yale University. After two years at the California Institute of Technology as an American Cancer Society Postdoctoral Fellow, she joined the faculty of the University of Wisconsin, Madison in 1991. In 2017, she returned to MIT as the Novartis Professor of Chemistry and Member of the Broad Institute. She is also a Member of the Koch Institute and an Associate Member of the Ragon Institute. Her interdisciplinary research interests have advanced our understanding of cell surface recognition processes, especially those involving protein-glycan interactions. Laura is a Fellow of the American Association for the Advancement of Science, and a Member of the American Academy of Microbiology, the National Academy of Sciences, and the National Academy of Medicine. She was the founding Editor–In-Chief of ACS Chemical Biology. Her honors and awards include a MacArthur Foundation Fellowship, a Guggenheim Fellowship, the ACS Gibbs Medal, the Tetrahedron Prize, the Centenary Prize of the Royal Society of Chemistry, and the Ronald Breslow Award for Achievement in Biomimetic Chemistry.

Hosted by Professor Erin Carlson and Professor Theresa Reineke

Professor Laura Kiessling
Department of Chemistry
Massachusetts Institute of Technology

Revealing Glycan Interactions in Health and Disease

The glycans that coat the surfaces of cells can change in health and disease. While many studies have demonstrated these changes in diseases ranging from cancer to inflammation to infection, the impact of these alterations on immune recognition is poorly understood. Deepening our understanding of how glycosylation is controlled and how cell-surface glycan recognition impacts immune responses could lead to new therapeutic approaches that influence immunity or tolerance. We are leveraging our knowledge of human proteins that recognize glycans and nucleic acid amplification strategies to generate new tools that can provide insight into how glycans shape immunity. This seminar will describe the application of these tools to elucidate the consequences of altered glycosylation in the context of infection and cancer. We anticipate that this approach can be used to identify novel strategies for combating diverse diseases.

Laura Kiessling

Laura Kiessling earned a BS in Chemistry from the Massachusetts Institute of Technology and a Ph.D. in Organic Chemistry from Yale University. After two years at the California Institute of Technology as an American Cancer Society Postdoctoral Fellow, she joined the faculty of the University of Wisconsin, Madison in 1991. In 2017, she returned to MIT as the Novartis Professor of Chemistry and Member of the Broad Institute. She is also a Member of the Koch Institute and an Associate Member of the Ragon Institute. Her interdisciplinary research interests have advanced our understanding of cell surface recognition processes, especially those involving protein-glycan interactions. Laura is a Fellow of the American Association for the Advancement of Science, and a Member of the American Academy of Microbiology, the National Academy of Sciences, and the National Academy of Medicine. She was the founding Editor–In-Chief of ACS Chemical Biology. Her honors and awards include a MacArthur Foundation Fellowship, a Guggenheim Fellowship, the ACS Gibbs Medal, the Tetrahedron Prize, the Centenary Prize of the Royal Society of Chemistry, and the Ronald Breslow Award for Achievement in Biomimetic Chemistry.

Hosted by Professor Erin Carlson and Professor Theresa Reineke

Donald Betz and Victor Sousa
Sherwin‐Williams

Innovating in a Corporate World

Innovation does not happen by accident; it is intentionally designed. As the world’s leading coatings company, Sherwin‐Williams must continuously operate at the forefront of innovation to remain competitive. “Innovating in a Corporate World” examines the foundational structures, mindset, and tools required to translate the Voice of the Customer into meaningful solutions. Recent product innovations within the Coil business unit serve as practical examples of how disciplined, customer‐driven innovation is successfully executed at scale.

Donald Betz

Donald Betz is the Senior Director of Innovation at Sherwin‐Williams, based in Cleveland, Ohio. In his role, he leads global innovation strategy across multiple business units. With over 25 years of experience in coatings R&D and innovation leadership, he focuses on translating customer needs into scalable, high‐impact solutions that deliver real business value. Donald holds a Bachelor of Science in Chemistry.

Victor Sousa

Victor Sousa is a Technical Manager for Coil Coatings at Sherwin-Williams, based in Minneapolis, Minnesota. He began his career at Sherwin-Williams in 2005 in Brazil, where he worked in technical and research roles supporting the development of coating technologies. In 2024, he relocated to the United States to continue his career within the company’s R&D leadership organization. Victor holds a Bachelor of Science in Chemical Engineering and a Master of Business Administration (MBA).