2012 Recipients

Eli Lilly Award in Biological Chemistry

Professor Christopher J. Chang, University of California, Berkeley.

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

Professor Christopher J. Chang is the recipient of the 2012 Eli Lilly Award in Biological Chemistry, in recognition of his contributions to discovery and understanding of new chemical signaling agents in biological systems. More specifically, Chang and his co-workers have developed molecular imaging probes that permit them to visualize the real-time production and/or trafficking of specific reactive oxygen species and metal ions in living cells and animals. These chemical tools have allowed the discovery and elucidation of new signal transduction pathways in a variety of models, including brain neurons, stem cells, adipocytes, cancer cells, and macrophages relevant to neurodegenerative and infectious diseases, cancer, diabetes, obesity, and regenerative medicine. For example, Dr. Chang has recently discovered that specific types of aquaporins, which are known to control the entry of water into cells and hence regulate osmotic pressure, can also function as channels for hydrogen peroxide, a molecule that is involved in redox signaling pathways. He will present a lecture as part of a symposium at the Fall 2012 ACS National Meeting.

Pfizer Award in Enzyme Chemistry

Professor Jin Zhang, Johns Hopkins University.

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

Professor Jin Zhang is the recipient of the 2012 Pfizer Award in Enzyme Chemistry, in recognition of her pioneering work in elucidating the spatiotemporal regulation of signaling molecules within the living cell. More specifically, she and her co-workers have developed novel genetically encoded fluorescent biosensors and applied them in living cells to track the activities of signaling enzymes such as protein kinases and phosphatases, which must be precisely regulated in both cellular space and time to perform their biological function. To date, these efforts have yielded an ever-expanding repertoire of fluorescent biosensors including reporters for PKA, PKC, Akt, c-jun N-terminal kinase, calcineurin, cAMP and phosphoinositides. Dr. Zhang’s laboratory has also devised new strategies to manipulate biochemical events inside living cells, which have served to unveil many of the molecular secrets underlying cell information processing, such as the identification of oscillatory kinase activities as a new mode of signal transmission. Her work is therefore establishing spatiotemporal regulation as a fundamental paradigm in cell signaling, with significant implications for (i) our understanding of both normal cell physiology and disease states, and (ii) enzyme function in living cells. She will present a lecture as part of a symposium at the Fall 2012 ACS National Meeting.

The Repligen Award in Chemistry of Biological Processes

Professor Carol Fierke, University of Michigan.

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

Professor Carol Fierke is the recipient of the 2012 Repligen Award in the Chemistry of Biological Processes, in recognition of her contributions to our broad understanding of how protein and nucleic acid catalysts achieve high efficiency with rigorous control of reaction specificity. In addition to her work on catalysis, Fierke and co-workers have made a number of significant contributions to our view of metal ion homeostasis in cells. She is recognized as an international leader in devising elegant experimental approaches for probing the structure, function and biological relevance of metals as cofactors in catalysis. More specifically, she and her co-workers carried out a groundbreaking analysis of the determinants of metal affinity and specificity for carbonic anhydrase, the prototypical zinc enzyme, and then used this information to develop biosensors to make the first real-time measurement of the cellular concentration of readily exchangeable zinc ions, thereby permitting them to analyze cellular zinc homeostasis. She has also identified the biological metal cofactor and elucidated the catalytic mechanism of several other metalloenzymes, including protein farnesyltransferase, histone deacetylase and ribonuclease P. These studies have often led to unexpected conclusions that change the field. For example, she showed that the substrate for the ribozyme catalyst in ribonuclease P, which is only active as a protein/RNA complex, was actually bound by the protein subunit in contrast to previous hypotheses. Her work has also led to the novel proposal that cells may regulate enzyme activity by switching metals in the active site. More recent efforts to identify and quantify the in vivo substrates of enzymes that catalyze post-translational modifications have enhanced our understanding of the role of these modifications in biological pathways. Her ability to integrate ideas and methods from a variety of scientific disciplines to determine fundamental details about catalytic activity and cellular function is a hallmark of Professor Fierke’s work, which is important for efforts to develop enzyme inhibitors as therapeutic agents. She will present a lecture as part of a symposium at the Fall 2012 ACS National Meeting.


Gordon Hammes ACS Biochemistry Lectureship

Professor Angela Gronenborn, University of Pittsburgh.

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 Angela Gronenborn will present the Gordon Hammes ACS Biochemistry lecture at the Fall 2012 National Meeting of the American Chemical Society, in recognition of her pioneering achievements in the development of NMR methodologies for the determination of biomolecular structure, and in their subsequent application to proteins of particular biological interest. More specifically, she played a key role in employing constrained molecular dynamics and simulating annealing strategies to generate protein structures from NMR-derived distance restraints, and she and her group were leaders in using multi-dimensional, heteronuclear spectroscopic methods to extend NMR methods for the study of higher molecular weight molecules. Her invention of a novel PCR-based approach to prepare DNA that is uniformly isotopically labeled on a large scale has facilitated the detailed study of both the structure and dynamical properties of this class of biopolymer. Using the techniques that she pioneered, Dr. Gronenborn has been able to solve the structures of many cytokines and chemokines, which play critical roles in cell-cell signaling, and many proteins that are relevant to the biology of human immunodeficiency virus (HIV), including cyanovirin N, which inhibits HIV infection. She has also sought to elucidate the structure and dynamics of transiently formed complexes that are critical for cellular regulation and signaling but which are not amenable to study by X-ray crystallography. This work includes the mechanical processes by which the interaction of the SRY protein with its target DNA sequence induces a kink into the DNA. Her efforts to develop and harness the power of NMR for studying the three-dimensional structure of large proteins have opened new vistas for research upon the relationship between structure, dynamics and biological function.

The ACS Chemical Biology Lectureship

Professor Carolyn Bertozzi, University of California, Berkeley.

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

Professor Carolyn Bertozzi will present the 2012 ACS Chemical Biology lecture at the Spring 2012 National Meeting of the American Chemical Society, in recognition of her numerous contributions to chemical biology, which bridge the gap between molecular chemistry and biological function. As a leading innovator in the field, she developed reagents for “bioorthogonal chemistry”, most notably those for Staudinger ligation and copper-free “click” chemistry, which permit chemists to carry out synthetic chemistry transformations within the complex chemical milieu that is present in cellular environments. These tools were originally designed to image cancer-specific cell-surface sugars, but their utility extends to many problems in chemical biology. For example, the Staudinger ligation chemistry has permitted her to perform advanced imaging studies in simple animal models, such as zebrafish, opening up new possibilities for understanding the spatial and temporal events that take place during growth and differentiation. Moreover, her development of a “genetically-encoded aldehyde tag” is a simple and elegant solution to the problem of site-specifically modifying protein structures in the cell, which is currently being commercialized to yield new protein-based therapeutics. Her tools have also revolutionized both the study of complex carbohydrates that decorate the cell surface and mediate cell-cell interactions, and provided chemists with the ability to “tag” specific molecules on the cell surface. Finally, she and her co-workers are trying to elucidate the biological functions of sulfated sugars, with a particular focus on the sulfotransferase enzymes that are used to assemble these molecules. Importantly, Professor Bertozzi has discovered that the properties of these enzymes are highly dependent on their location in specific regions of the cell, and recent work upon sulfur metabolism during mycobacterial infections has allowed her to identify a promising new target for the development of therapeutics against tuberculosis.

Murray Goodman Memorial Prize

Professor Jeffrey Kelly, The Scripps Research Institute.

For contributions.

The 2012 Goodman Award, sponsored by Biopolymers is awarded to Jeffery Kelly. The symposium for this award will be held at the Fall ACS meeting in Philadelphia in August 2012

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

dougherty

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