Past Recipients

2011 Recipients

Eli Lilly Award in Biological Chemistry

Professor Nathanael Gray, Harvard University.

For outstanding research in biological chemistry of unusual merit and independence of thought and originality.

Professor Nathanael Gray is the recipient of the 2011 Eli Lilly Award in Biological Chemistry, in recognition of his success in executing multi-disciplinary drug discovery strategies within an academic setting. More specifically, Professor Gray and his co-workers have developed new kinase inhibitors that permit them to elucidate the relevance of a given kinase in physiological and pathophysiological processes. These efforts have not only allowed them to make major contributions to our general understanding of novel approaches for kinase inhibition but also to discover the first allosteric inhibitors of Bcr-Abl (GNF-2 & 5), develop the first mutant specific inhibitors of T790M EGFR (WZ-4002) and identify the first potent inhibitors of EML4-ALK (TAE684), mTor (Torin1), Mps1 (Mps1-IN-1) and Erk5 (XMD8-92). Because all of these proteins become deregulated in cancer, these findings are likely to be translated into valuable new therapies. Professor Gray’s work is unique in the chemical community in that he is dedicated to optimizing the potency, selectivity and pharmacological properties of his allosteric inhibitors to the point that they become generally useful as research tools or as potential drug candidates. He will present a lecture as part of a symposium at the Fall 2011 ACS National Meeting.

Pfizer Award in Enzyme Chemistry

Professor Sarah O’Connor, Massachusetts Institute of Technology.

For outstanding work in enzyme chemistry where the presence of enzyme action is unequivocally demonstrated.

Professor Sarah O’Connor is the recipient of the 2011 Pfizer Award in Enzyme Chemistry, in recognition of her pathbreaking contributions to understanding the enzymological and chemical logic of monoterpene alkaloid biosynthesis. In recent years her group has made inroads into the mechanistic understanding of key biochemical transformations observed in plant alkaloid biosynthesis, and in parallel with these efforts, she has been able to re-engineer the substrate specificity of several alkaloid biosynthetic enzymes. In an important advance for the reprogramming of plant biosynthetic pathways, Professor O’Connor and her co-workers have used these modified enzymes in metabolic engineering efforts, which has led to the successful use of plant tissue for the production of novel product structures. This success sets the stage for future efforts to obtain “unnatural” plant natural products with improved pharmacological properties. Professor O’Connor is also recognized for her role in a large-scale project aimed at generating a transcriptomics and metabolomics database that will provide a modern resource for understanding and elucidating medicinal plant natural product biosynthetic pathways. This work has already led to the discovery of a previously uncharacterized gene involved in vinblastine biosynthesis. She will present a lecture as part of a symposium at the Fall 2011 ACS National Meeting.

The Repligen Award in Chemistry of Biological Processes

Professor Richard Armstrong, Vanderbilt University.

For outstanding contributions to the understanding of biological processes with particular emphasis on structure, function and mechanism.

Professor Richard Armstrong is the recipient of the 2011 Repligen Award in Chemistry of Biological Processes, in recognition of his contributions to our understanding of detoxification enzymes within the cell. Some of the highlights of these efforts include the determination of the first crystal structure of a glutathione transferase with glutathione bound, the elucidation of the chemical and kinetic mechanisms of epoxide hydrolases with single-turnover and rapid kinetic experiments, the first evaluation of conformational changes in integral membrane proteins (microsomal glutathione transferases and cytochrome c oxidase) by amide H/D exchange mass spectrometry, and the discovery of multiple enzymatic mechanisms for the resistance of pathogenic microorganisms to the antibiotic fosfomycin. His most recent work has been directed at the discovery of new enzyme function and extent of functional diversity in the glutathione transferase superfamily. A hallmark of Professor Armstrong’s work has been his ability to integrate of ideas and methods from multiple scientific disciplines to illuminate the molecular basis of complex biological processes. These disciplines include physical organic chemistry, enzymology, structural biology, spectroscopy, computational chemistry, bioinformatics and more recently functional genomics. In addition to his scientific achievements Professor Armstrong has a substantial record of professional service and has been Editor-in-Chief of the journal Biochemistry since 2004. He will present a lecture as part of a symposium at the Fall 2011 ACS National Meeting.

Murray Goodman Memorial Prize

Professor Dennis A. Dougherty, California Institute of Technology

For outstanding accomplishments in one or more of the areas of biochemistry, biophysical chemistry, biophysics, and/or chemical biology
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Professor Dennis A. Dougherty received his B.S. and M.S. degrees from Bucknell University in 1974. He did his doctoral research at Princeton University with Kurt Mislow and a year of post-doctoral studies with Jerome Berson at Yale University. Dougherty joined the faculty in the Division of Chemistry and Chemical Engineering at the California Institute of Technology in 1979, where he is now the George Grant Hoag Professor of Chemistry.

Dougherty is perhaps best known for development of the cation-π interaction, a novel but potent binding interaction between molecules that plays a central role in establishing protein structures and in modulating drug-receptor interactions. The fundamental nature of the interaction was established through extensive theoretical and model studies by the Dougherty group. Dougherty also established the prevalence of the cation-π interaction in biological systems, and it is now recognized to be important in a wide range biological processes.

More recently, Dougherty has addressed molecular neurobiology, applying the mindset and tools of physical organic chemistry to the complex proteins of neuroscience – the molecules of memory, thought, and sensory perception; of Alzheimer’s, Parkinson’s, and schizophrenia. Target receptors include the nicotinic acetylcholine receptor, the 5-HT3 (serotonin) receptor, and the D2 dopamine receptor. Through these efforts, Dougherty has produced fundamental insights into drug-receptor interactions, including cation-π interactions.

Dougherty is a member of the National Academy of Sciences and a fellow of the American Association for the Advancement of Science and the American Academy of Arts and Science. He has been recognized with a number of awards, including the ACS James Flack Norris Award for Physical Organic Chemistry, the Hoffmann Medal of the University of Zurich, the Tolman Medal (2010), the AstraZeneca Excellence in Chemistry Award, the Arthur C. Cope Scholar Award, and has been designated a Javits Neuroscience Investigator by NIH. He is also the co-author, with Professor Eric Anslyn, of the influential textbook, Modern Physical Organic Chemistry.

  • Previous Goodman Award Recipients (Coming Soon)

Gordon Hammes ACS Biochemistry Lectureship

Professor Doug Turner, University of Rochester.

For outstanding contributions in scientific research at the interface of chemistry and biology, particularly in the realm of biochemistry, biological chemistry and molecular biology.

Professor Doug Turner will present the 2011 Gordon Hammes ACS Biochemistry lecture at the Fall 2011 National Meeting of the American Chemical Society, in recognition of his pioneering contributions to elucidating the rules that relate RNA sequence to the stability of RNA structures. Professor Turner is the recognized world authority on the prediction of RNA secondary structure and pioneered the use of rigorous thermodynamic measurements to quantify the contributions of individual base pair hydrogen bonding and base pair stacking interactions within a given sequence context to the stability of folded RNA in water. These studies have culminated in the freely available web-based computer program, mfold (created by Michael Zuker), that permits investigators to determine and compare the stability of different possible structures of folded RNA, which has had a significant worldwide impact on our understanding of RNA function. In addition, Professor Turner has carried out groundbreaking work on the elucidation of DNA and RNA folding pathways using rapid kinetics, and has made major contributions to our knowledge of structural motifs that are commonly found in RNA, such as stable “tetraloops” and tandem G-A base pairs. More recent studies have focused on understanding how the introduction of “Locked Nucleic Acids” (LNAs) into RNA duplexes elevates their melting temperature. With typical rigor, Professor Turner and his co-workers have been able to divide the effect on melting temperature into individual thermodynamic contributions. These efforts to gain fundamental insights are essential to developing therapeutic applications for LNAs that exploit their ability to bind micro-RNAs and block their cellular action.

The ACS Chemical Biology Lectureship

Professor Stuart Schreiber, Harvard University.

For contributions that have had a major impact on scientific research in the area of Chemical Biology.

Professor Stuart Schreiber will present the 2011 ACS Chemical Biology lecture at the Spring 2011 National Meeting of the American Chemical Society, in recognition of his pioneering contributions to research at the interface of chemistry and biology. As one of the early innovators in developing a vision of how small molecules might serve as tools in biological discovery, he has applied the methodologies of synthetic organic and physical organic chemistry to solve problems in molecular and cellular biology. Indeed, it might be said that no individual has done more to bridge the philosophical divide between chemists and biologists. Beginning with his identification of the protein FKBP as the target for the immunosuppressant FK506 and its role in T-cell signaling, he and his co-workers have gone on to pioneer the concept of diversity-oriented synthesis and “chemical genetics” to discover new drug targets and to elucidate new biological pathways, including the fundamental biological importance of histone deacetylation. His current work deals with exploiting new insights into cancer cell genomes to develop novel therapeutic agents by correlating small molecule efficacies with the genetic features of human cancers.

The Molecular BioSystems Award

Professor M. Madan Babu, MRC Laboratory of Molecular Biology, Cambridge, UK.

For significant contributions to the fields of Chemical Biology, the “omics” sciences and Systems Biology.

Dr. Madan Babu is the recipient of the 2011 Molecular Biosystems Award , in recognition of his contributions to our understanding of the regulatory networks employed by cells and the application of these fundamental ideas to systems biology. His accomplishments are widely recognized in the community even though he is at an early stage in his independent research career. As a computational biologist, Dr. Babu has sought to model the complexity of cellular networks, which are critical to regulating gene transcription in eukaryotes and to elucidate how the requirements of these signaling pathways have impacted their evolution. His analyses have also provided new insights in the dynamical properties of these regulatory networks. A hallmark of his work has been the development of innovative methodologies to facilitate analysis of the very large data sets generated in experimental high throughput “omics” research. He will present a lecture as part of a symposium at the Spring 2011 ACS National Meeting.

The Founders Travel Award

Dr. Paul Cook, Vanderbilt University.

To support the participation of students and/or postdocs at the Winter Enzyme Mechanisms Conference.

Dr. Paul D. Cook (Vanderbilt) was selected as the recipient of the second Founders Travel Award. This award was presented to Dr. Cook on January 4, 2011 at the 22ndmeeting of the Winter Enzyme Mechanisms Conference in St Pete Beach, Florida. Dr. Cook completed his Ph.D. with Hazel Holden at the University of Wisconsin-Madison, and then moved to become a postdoctoral fellow with Richard Armstrong at Vanderbilt University. The audience at this conference paid close attention to Paul’s stimulating talk on “Structure/Function Studies of the Fosfomycin Resistance Enzyme FosB”.

  • Previous Founders Travel Award Recipients