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Meet the ACS Chemical Biology Early Career Board.

ACS Chemical Biology is excited to announce its first Early Career Advisory Board appointments. This inaugural board features 25 young researchers with an impressive variety of expertise from across the globe. They will work with the journal’s Editor-in-Chief, Laura L. Kiessling, and its Associate Editors to share their experiences and perspectives on emerging topics within the chemical biology community.

Get to know the members of the ACS Chemical Biology Early Career Board.

Kerriann Backus, UCLA

What’s your background?

I received a B.S. in Chemistry and a B.A. in Latin American Studies in 2007 from Brown University. My doctoral research was conducted in the laboratories of Benjamin Davis (Oxford) and Clifton Barry (NIH, NIAID) as a 2007 Rhodes Scholar and an NIH Oxford Cambridge Scholar. My Ph.D. work focused on the development of chemical probes to label and image Mycobacterium tuberculosis. In 2012, I completed my doctorate and began an NIH postdoctoral fellowship at The Scripps Research Institute in the laboratory of Benjamin Cravatt. My postdoctoral research developed chemoproteomic methods for the proteome-wide identification of ligandable cysteine and lysine residues. At UCLA, my research has been recognized by numerous awards, including a Beckman Young Investigator, DARPA Young Faculty Award, a V Scholar Research Award, and a Packard Fellowship.

What are you currently working on?

The Backus lab integrates chemoproteomic methods with genomics and genetics tools to enable the rapid and proteome-wide identification of functional and potentially ‘druggable’ cysteine and lysine residues.

What do you hope to bring to the journal?

I hope to bring strong expertise in chemical probes and chemoproteomic methods to the journal. What I hope to see more of in ACS Chemical Biology is more technology development and interdisciplinary multi-omic methods.

What’s the most interesting challenge in your field at the moment?

Deciphering the functions of the thousands of ligandable residues across the proteome.

Jeremy Baskin, Cornell University

What is your background?

My training is in bioorthogonal chemistry, chemical glycobiology, and the cell biology of lipids and membranes. My Ph.D. work from Professor Carolyn Bertozzi’s lab at University of California at Berkeley focused on developing cyclooctyne reagents for bioorthogonal strain-promoted azide-alkyne cycloadditions and their application to in vivo imaging of glycans in developing zebrafish. My postdoctoral work from Professor Pietro De Camilli’s lab at the Yale School of Medicine centered on elucidating mechanisms controlling phosphoinositide synthesis at the plasma membrane and their role in the etiology of genetic diseases of the brain white matter.

What are you currently working on?

My lab at Cornell University operates at the interface of chemical biology and cell biology. We are fascinated by how cells produce specific lipids to control diverse signaling events. We are developing chemical tools to understand these phenomena, including new bioorthogonal metabolic probes and light-controlled, optogenetic enzymes, to visualize and perturb phospholipase D and phosphatidic acid signaling. We are also probing new mechanisms by which phosphoinositide lipids affect signaling in the cell by engaging and regulating lipid-binding proteins’ action. Our work has collectively shed light on how cells use these lipids to regulate pathways, including Wnt signaling and Hippo signaling in normal physiological and pathological contexts, including in cancer.

What do you hope to bring to the journal?

I am excited to bring to ACS Chemical Biology my perspectives from “both sides of the aisle,” as someone who is equally passionate about innovative chemical methods for observing important phenomena to generate new hypotheses and question-driven investigations to elucidate critical mechanisms in biological systems. I am committed to helping the journal broaden and diversify its reach, which encompasses both a diversification of scientific topics and promoting diversity in its key stakeholders — authors, reviewers, editors, readers — to best serve the community of chemical biologists.

What’s the most interesting challenge in your field at the moment?

In the world of lipid signaling, major challenges include developing tools to accurately track where specific lipids are produced in the cell and how they get shuttled from one membrane to the next. Equally important is sorting out the signal from the noise, that is, figuring out which lipids are the drivers of specific signaling events versus ones that are present but not the main actors in a particular physiological response. These challenges necessitate developing highly precise visualization tools and perturbation and physiologically relevant assays to probe biological mechanisms. I think they are perfectly emblematic of a 21st-century chemical biology problem: right at the interface of tools development and biological discovery.

George M. Burslem, University of Pennsylvania

What’s your background?

I completed my undergraduate degree in chemistry at the University of Bristol before moving to the University of Leeds for grad school. At Leeds, I worked in the labs of Professor Andrew Wilson and Professor Adam Nelson on inhibitors of protein-protein interactions. After graduating, I moved to the Department of Molecular, Cellular and Developmental Biology at Yale University to work with Professor Craig Crews as a Fellow of The Leukemia & Lymphoma Society working on targeted protein degradation. In 2020, I established my lab at the Perelman School of Medicine, University of Pennsylvania.

What are you currently working on?

My lab is interested in developing chemical tools to understand and modulate lysine post-translational modifications, specifically acetylation and ubiquitination. The laboratory is particularly interested in novel pharmacological approaches to modulate post-translational modifications that regulate gene expression and protein stability.

What do you hope to bring to the journal?

I hope to continue building a community of chemical biology researchers around the journal and highlighting early-career investigators’ work, including the graduate students and post-docs behind the papers. I would also love to highlight the power of chemical biology to our biological colleagues.

What’s the most interesting challenge in your field at the moment?

I think the most interesting challenge is always identifying new biological questions that can’t be answered using traditional approaches and then developing new chemical tools to answer them. For me, that might be orthogonal methods for targeted protein degradation or tools to break the ubiquitin code.

Chandrima Das, Saha Institute of Nuclear Physics, Kolkata

What’s your background

I completed my B.S. in Chemistry (Hons.) and M.S. in Biochemistry (Specialization: Molecular Biology) from University of Calcutta in 1996 and 1999, respectively. I obtained my Ph.D. from Jawaharlal Nehru Centre for Advanced Scientific Research (JNCASR), Bangalore, India, in 2007, with a specialization in chromatin structural regulation by Nonhistone Chromatin Associated Protein (NCAP). I performed my postdoctoral research at University of Colorado Denver (2008-2010) and M D Anderson Cancer Center (2010-2012) on the discovery and functional characterization of a novel human epigenetic mark, H3K56Ac. I was awarded Susan G. Komen Postdoctoral Fellowship for basic sciences in Breast Cancer Research (2009).

In summer 2012, I joined as a faculty member in Saha Institute of Nuclear Physics (SINP) and established the Chromatin Dynamics Laboratory. My focus has been on the modulation of chromatin structure by selective epigenetic recognition by a class of proteins entitled chromatin “reader/effector.” We are trying to understand these chromatin-binding transcription factors’ diverse functions to dictate the on/off state of the underlying genes in different physiological conditions and pathological states like cancer, metabolic, and infectious diseases. I have received prestigious Research Grants funded by Govt. of India, including Ramalingaswami fellowship from Department of Biotechnology (2011-12), Swarna Jayanti Fellowship from Department of Science and Technology (2017-18), and S. Ramachandran – National Bioscience Award for Career Development – 2019, from Department of Biotechnology, Govt. of India.

I have been elected as a member of the West Bengal Academy of Science and Technology (WAST). This society promotes basic and applied science and technology in West Bengal, India. I am also the Life Member of Indian Society of Cell Biology (ISCB), Indian Association for Cancer Research (IACR), Society of Biological Chemists (SBC), India, Chemical Biology Society (CBS), India, and a Member of The American Society for Biochemistry and Molecular Biology (ASBMB). Recently, I have been nominated as a member of The ACS Chemical Biology Early Career Board.

What are you currently working on?

We have started a vibrant research group in the Biophysics & Structural Genomics Division, Saha Institute of Nuclear Physics, Kolkata, India. Our group focuses on understanding the fundamental mechanisms of epigenetic deregulation of genes in human diseases and has made several seminal contributions in the field. In this context, we are working on a specific class of proteins called chromatin “readers/effectors,” which are known to impact the epigenetic mechanisms in normal conditions as well as diseased states.

Our laboratory’s research work includes the role of epigenetic readers in tumorigenicity. Breast cancer is one of the major causes of mortality in females. The heterogeneity of the disease is a therapeutic challenge. Through early diagnosis, breast cancer has been challenged with conventional therapies, including chemotherapy, radiation therapy, hormonal therapy, and surgery. Complexities arise with a particular subtype of the disease, which is Triple-Negative Breast cancer (TNBC), as this particular subtype is the most aggressive and therapy non-responsive form of the disease, with potential chances of relapse. In this context, our laboratory is working on an important chromatin reader protein Zinc Finger MYND (Myeloid, Nervy, and DEAF-1)-type containing 8 (ZMYND8). ZMYND8 has been shown to harbor conventional CHD4-independent functions in regulating gene expression through its modified histone binding ability (J Biol. Chem., 2016).
Further, ZMYND8 has been shown to suppress tumorigenicity through independent molecular mechanisms: (i) Positive regulation of epithelial gene expression programs (Biochemical Journal, 2017), (ii) Negative regulation of tumor-promoting gene expression programs (Cell Death & Disease, 2020), and (iii) Induction of cellular differentiation programs (J. Biosciences, 2020). Interestingly, the role of ZMYND8 in modulating retinoid-based therapy (as an All trans-retinoic acid-responsive transcription factor) opens up new avenues to combat tumor growth through an epigenetic perspective (BBA Gene Regulatory Mechanisms, 2017). Apart from this classical chromatin reader protein, we are also investigating the newly acquired functions of chromatin reader family members.

In this regard, we have recently identified that Plant Homeo Domain (Ph.D.) finger protein Ubiquitin Protein Ligase E3 Component N-Recognin7 (UBR7) has enzymatic catalytic activity. We have established that UBR7 has a novel histone H2B monoubiquitin ligase that suppresses tumorigenesis and metastasis in TNBC through modulating Wnt/β-Catenin signaling pathway (Nat Commun. 2019). Interestingly, we have also identified a novel substrate of chromodomain family protein CBX4/Pc2, which has an important role in tumorigenicity. For the first time, we show that hTERT is SUMOylated by SUMO E3 ligase CBX4 and promotes breast cancer migration and invasion (Biochem J., 2020). Apart from the mainstream research interest from our laboratory, we are also involved in collaborative projects on therapeutically important small molecules as regulators of epigenetic modifications.

What do you hope to bring to the journal?

The scope of interdisciplinary research in the field of biological science is ever-growing. Being trained in chemistry, followed by Biochemistry in Bachelors and Masters respectively, has led to a better appreciation of several interface problems in biology.ACS Chemical Biology provides an opportunity to facilitate both the biologists and chemists to translate their discoveries for a wider audience. Ranging from in vitro methods to ex vivo cell biological questions and finally validating the proof of concepts in vivo in the organismal models are enthusiastically encouraged in this journal. Having an overall understanding of these systems would help me contribute towards welcoming new research in epigenetics and chromatin biology, which is a contemporary area of active research globally. Further, being an active member of the editorial board could bring special advanced focused issues into fruition.

What’s the most interesting challenge in your field at the moment?

Epigenetic modifications of chromatin fine-tune the underlying gene expression programs and are causally related to the organism’s normal homeostasis and the pathobiological state. The epigenetic modifications are operated through a class of proteins termed as “chromatin reader/effector,” which lead to differential recruitment of other regulatory factors (including writers and erasers) to specific sites leading to activation/repression of gene expression. The epigenetic code created by the writer, reader, and eraser is complex and highly dynamic. Interpreting this epigenomic landscape has always been a challenging field of research. With the advent of CRISPR-Cas9 advanced genome editing system, it is possible to program this complex landscape in a more targeted manner. The major challenge would be to introduce gene-specific epigenetic alterations to make the transcription programs amenable to molecular cues given to the systems. Once we can program these genes by engineering the epigenomic landscape, the basic understanding and restoration of the disease states’ molecular scenario would be possible in the future.

Laura Dassama, Stanford University

Coming Soon!

Yael David, Sloan Kettering

What’s your background?

I received my B.S. in Biology from SUNY Stony Brook as a Summa Cum Laude. I was awarded the Howard Hughes Medical Institute Fellowship to perform molecular neurobiology research with Professor Lonnie Wollmuth.

I subsequently moved to the Weizmann Institute of Science in Israel, where I performed my graduate work with Professor Ami Navon at the direct Ph.D. track. There, I was trained as a biochemist, applying my knowledge to study polyubiquitination mechanisms and regulation. Realizing the power of interdisciplinary research, I moved to the Chemistry Department at Princeton University, where I combined my experience in cell biology and biochemistry with Professor Tom Muir’s expertise in peptide chemistry to develop novel tools towards the mechanistic investigation of histone post-translational modifications, including their site-specific manipulation in live cells. This methodology opened the door to performing research with chemical precision at a biochemical resolution and in a physiological context.

In September 2016, I brought my powerful program to the Chemical Biology department at Memorial Sloan Kettering Cancer Center to focus on cancer research. My lab has performed highly innovative and interdisciplinary research driven by outstanding questions in the Epigenetics field in the past four years. We developed key chemical tools that were applied, among others, to identify a new class of histone modifications that directly links metabolism and cell fate. My efforts thus far were recognized nationally and internationally as the ACS “future of biochemistry,” “rising start in chemical protein synthesis,” the Pershing Square Sohn Cancer Alliance award, the Parker Institute for Cancer Immunotherapy Career Award, and the NIH/NIGMS outstanding young investigators award, MIRA, among others.

What are you currently working on?

My lab’s research efforts apply core chemical biology, biochemistry, and cell biology techniques to address fundamental questions in transcription’s epigenetic regulation. Epigenetic regulation relies on the dynamic modification of the two building blocks of chromatin: DNA and histone packaging proteins, to establish and maintain cell identity and fate. We develop and utilize chemical methods to track, manipulate, and synthesize site-specifically modified histones in vitro and in vivo and study the roles that these modifications play in disease states, with the ultimate goal of targeting them therapeutics.

What do you hope to bring to the journal?

As a trained biologist who transitioned to chemical biology later in my career and ran a lab at a biomedical institute, I hope to bring a young and fresh perspective that may appeal to people of different backgrounds. Together with an innovative and multidisciplinary perspective, I hope to bridge fields and expertise, as well as academia and industry.

What’s the most interesting challenge in your field at the moment?

The field of chemical biology has been in a growth phase over the last couple of decades, but these last five years have seen the field move into hyperdrive. This transition is fueled by the huge technological leap in high throughput methodologies, quantitative proteomics, and genetic editing that enable the precise identification of new targets, the development of new ways to modulate them, and the capacity to determine the effect of the manipulation. However, we believe that the major conceptual transformation in chemical biology is in the types of questions these technologies aim at, which are becoming more translational to enable drug discovery. Chemical biology is thus pioneering a new bridge between academia and industry. Importantly, chemical biologists are becoming more focused on asking impactful biological questions and more fearless in their pursuit of understanding complex cellular mechanisms.

Over the last few years, there has been a surge in academic labs spinning out startup companies based on chemical biology-based technologies such as Vividon using chemoproteomic discoveries from the Cravatt Lab, Palleon that exploits glycol-immunobiology from the Bertozzi Lab, or Arvinas using the PROTAC technology from the Crews lab just to name a few. Large pharma companies have been building chemical biology departments to impact their drug pipelines and enable discovery efforts. These days, it is very common to see research conferences packed 50/50 with academic and industry scientists chasing similar goals.

One great example is the popular Bioorganic GRC meeting that is typically co-chaired by an academic P.I. and industry scientist, and equal attendance from both often lead to fruitful collaborations. For this upward trend is to continue, the next five years will be critical to deepening the intimate interaction between industry and academia. Given the complexity of biology, strengthening collaborations between industry and academic labs will be key over the next five years to continue this upward trajectory. Education of chemical biology trainees is also going to be important to teach and enable students to ask impactful biological questions, employ appropriate research strategies, and know-how to effectively communicate and work well with the diverse scientific backgrounds in the chemical biology melting pot.

This can be done through exposure to industrial components inside academic hubs, such as the WCM/MSKCC/RU Tri-Institutional Therapeutic Discovery Institute (TDI), establishing incubator hubs for accelerating startup companies, or through collaborations with pharma/biotech companies. We believe that chemical biology can serve as a powerful bridge between academia and industry that facilitates the synergistic impact on our fundamental understanding of pathological events and our capacity to treat them.

Laura Edgington-Mitchell, University of Melbourne

What’s your background?

I grew up on a goat farm in rural Kentucky before completing my bachelor’s degree in biology and chemistry at Transylvania University. Excited by the prospect of using chemistry to study biology, I enrolled in a doctoral program in the laboratory of Prof Matthew Bogyo at Stanford University (2007-2012). During that time, I began to develop chemical probes to study proteolytic enzymes in cancer and inflammation. For my postdoctoral studies, I packed up my chemical toolkit and moved to Melbourne, Australia. I applied my probes to study proteases in breast cancer metastasis at La Trobe University and then in inflammatory bowel diseases at Monash University. In 2018, I established the Protease Pathophysiology Lab at the Bio21 Institute within The University of Melbourne.

What are you currently working on?

I continue to maintain an interest in all things involving proteases. I work with chemists to diversify the available tools to study cysteine and serine proteases by imaging, proteomics, and other biochemical methods. I am applying these tools to study proteases’ contribution to gastrointestinal diseases, host-pathogen responses, cancer metastasis, and pain mediated by protease-activated receptors. My lab’s overarching goal is to establish proteases as biomarkers and therapeutic targets that will aid in the diagnosis and treatment of these diseases.

What do you hope to bring to the journal?

I have experience working in academic labs in two different countries/continents and across two very different systems. I also collaborate widely internationally and have worked with industry. This unique perspective will hopefully be a valuable addition to the journal.

What’s the most interesting challenge in your field at the moment?

There are more than 500 proteases in the human proteome. We have effective probes and inhibitors for only a small subset of these enzymes. Achieving specificity has proven difficult due to proteases having overlapping substrate preferences or very broad reactivity. New proteomics techniques provide more information about protease specificity, and novel screening techniques afford greater chemical diversity access. As such, the number of proteases that we can effectively target with chemical tools is rising.

Stephan Hacker, Technical University of Munich

What’s your background?

I studied Life Science at the University of Konstanz, Germany. I performed my doctoral research in Professor Andreas Marx’s group, working on synthesizing and applying fluorogenic probes to study nucleotide-dependent enzymatic processes. Afterward, I moved to the group of Professor Benjamin Cravatt at The Scripps Research Institute, La Jolla, California, where I developed chemical proteomic technologies to study the target engagement of lysine-directed covalent inhibitors with residue-specific resolution in a proteome-wide setting.

Since 2017, I am a group leader at the Technical University of Munich, Germany, where my group designs and synthesizes novel covalent inhibitors and uses them in phenotypic screenings and chemical proteomic experiments to identify new druggable targets proteins for antibiotics. My research focuses on the interface of chemistry and biology and develops novel chemical tools to better understand biological systems.

What are you currently working on?

My group’s current focus is to identify new target proteins for antibiotics that can be exploited to overcome the current health crisis caused by infections with antibiotic-resistant bacteria. For this purpose, my group is developing novel covalent inhibitors that allow us to target a diverse set of proteinogenic amino acids to broaden the applicability of covalent inhibitors to the vast majority of proteins. Furthermore, my group develops chemical proteomic technologies to use these protein ligands to globally understand which binding pockets in bacterial proteins are most suitable for targeted with covalent inhibitors. In this way, we identify prime candidates for the development of antibiotics with entirely new modes-of-action.

What do you hope to bring to the journal?

By joining the Early Career Board of ACS Chemical Biology, I hope to bring the specific challenges and needs of young independent investigators during the publication process into the journal’s focus.

What’s the most interesting challenge in your field at the moment?

In antibiotic discovery, overcoming the development of bacterial resistance to all marketed antibiotics by finding compounds with new mechanisms-of-action is one of the key challenges for the future. Finding compounds that can accumulate in the most challenging Gram-negative bacteria is a very important point to address in this context. In covalent inhibitor development, I am convinced that one key challenge is to find covalently reactive groups that selectively target diverse amino acids to address the multitude of important protein binding pockets that do not have a suitable cysteine residue.

Doris Hoeglinger, University of Heidelberg

What’s your background?

I’ve started as a chemist and, for a while, thought about going towards material science. But, luckily, I went to a biological institute for my master thesis, and my fantastic advisor introduced a multitude of biological questions that can be answered by often creating neat and elegant chemical tools. I was hooked and decided to pursue this further with a Ph.D. in biology, where I got interested in lipids’ biology, a topic that still fascinates me today.

What are you currently working on?

Our group studies lipid transport between organelles with a particular focus on the lysosome. To this end, we’re creating functionalized lipid probes that can be released inside living cells with a flash of light. Following their paths through the cell, we’re hoping to understand the basic biology of lipid homeostasis and their relevance in diseases such as lysosomal storage disorders.

What do you hope to bring to the journal?

I appreciate the opportunity to bring the perspective of an early career researcher and personally am glad to serve on a board that is also committed to highlighting the importance of diversity at every academic career stage. Scientifically, while I always appreciate the development of new chemical tools, I’m particularly interested in how their application allows one to answer previously inaccessible biological questions and how this opens up exciting new avenues of research.

What’s the most interesting challenge in your field at the moment?

In lipid biology, I think the biggest enigma is still to understand why there are so many different lipids. The cell invests a great deal of energy to make, distribute, and control thousands of different species’ levels. What are their individual functions, and how are they integrated into signaling processes? Here, the challenges mostly lie in finding the right tools to manipulate and follow the lipids of interest in their native environment.

Luca Laraia, DTU (Kopenhagen)

What’s your background?

I carried out a M.S. at Imperial College London, U.K., specializing in synthetic organic chemistry before moving to the University of Cambridge to carry out a Ph.D. in chemical biology. Here I focused on small molecule modulators of mitosis and DNA repair.

Following this, I moved to the Max Planck Institute of molecular physiology in Dortmund, Germany, where I focused on identifying small molecule modulators of autophagy and their targets using phenotypic screening, synthetic chemistry, and chemical proteomics. This led to new probes targeting lipid kinases, mitochondrial respiratory complexes, lipid transfer proteins, and lysosomal targeted agents. During my time at the MPI I was also involved in developing the pseudo-natural product concept to design and synthesize natural-product derived and inspired compound collections.

What are you currently working on?

My group is focused on the chemical biology of sterol-mediated processes. In practice, this involves the synthesis and biological evaluation of sterol-inspired and derived small molecules. In this context, we are actively looking to identify selective inhibitors of cholesterol transport proteins and are leveraging the power of targeted protein degradation in the field of cholesterol biosynthesis, metabolism, and transport. Our lab is a multidisciplinary environment combining synthetic chemistry, phenotypic screening, and cell biology, as well as chemical proteomics.

What do you hope to bring to the journal?

As one of the non-U.S. based researchers on the ECB, I hope to bring outside perspective to an ACS journal to widen the breadth of dialogue and ideas. I also hope to bring a synthetic and medicinal chemist’s view on a range of topics!

What’s the most interesting challenge in your field at the moment?

Cholesterol transport proteins are already reported to play roles in many processes, including, but not limited to, mediating organelle contact sites, autophagy, and viral entry. Developing selective tools to decouple their cholesterol transport function from other roles will help unravel their complex biology and provide potential therapeutics against a range of conditions.

Lingyin Li, Stanford University

Coming Soon!

Samira Musah, Duke University

Coming Soon!

Jia Niu, Boston College

What’s your background?

I received my B.S. and M.S. from Tsinghua University in China before moving to the U.S. to pursue a Ph.D. degree at Harvard University, working with Professor David Liu. After the doctoral study, I worked as a postdoctoral scholar with Professor Craig Hawker and Professor Tom Soh at U.C. Santa Barbara, before starting an independent faculty position at Boston College in 2017.

What are you currently working on?

My group focuses on three main thrusts: sustainable plastics, sulfated glycomimetics, and genomic editing. In the first direction, we are developing new strategies based on energetically favored cascade reactions to drive the polymerization or depolymerization of difficult synthetic and bio-derived monomers. In the second direction, we are developing new small molecule and macromolecular probes with defined sulfation patterns to study how sulfation as a chemical code function in signaling transduction. In the third direction, we are developing CRISPR genomic editors for programmable editing of genes and associated proteins through rational design and directed evolution approaches.

What do you hope to bring to the journal?

I hope to bring to the journal the perspective of a synthetic polymer chemist who is also interested in chemical biology and who sees synthetic polymers and biopolymers as unified “macromolecules” which functions range across biology and materials science.

What’s the most interesting challenge in your field at the moment?

There are three big questions I am most fascinated by:

  1. Can sustainable plastics be made out of renewable resources from biology and be 100% recycled?
  2. Beyond nucleic acid and protein, are there other molecularly patterned biomacromolecules that encode critical biological information? If there are, how is the information being written, edited, and read?
  3. For the biomacromolecules in (2), how can we develop synthetic systems to write, edit, and read the information to influence biology?

Sungwhan F. Oh, Brigham and Women's Hospital and Harvard Medical School

What’s your background?

I work in analytical chemistry and metabolomics.

What are you currently working on?

Bioactive metabolites originated from symbiotic microbiota and their host modulatory functions.

What do you hope to bring to the journal?

Experience in multifaceted natures of the field (on the interface of chemistry and biology).

What’s the most interesting challenge in your field at the moment?

Novel structure-function, biosynthesis, host-microbiota co-metabolism.

Emily Que, University of Texas, Austin

Coming Soon!

Vishal Rai, IISER Bhopal

What’s your background?

Chemical biology, bioconjugate chemistry, and organic chemistry.

What are you currently working on?

Chemical technologies for precision engineering of native proteins, antibody-drug conjugates, precision therapeutics.

What do you hope to bring to the journal?

The journal wants to bring the chemical biology community together and help in the field’s sustainable growth. I hope to join the team members and contribute positively to this mission.

What’s the most interesting challenge in your field at the moment?

How can we precisely engineer or target proteins? This question’s answer can address the technological demands of biotechnology, protein-based therapeutics, and precision therapeutics with covalent inhibitors.

Pablo Rivera-Fuentes, EPFL

What’s your background?

I got a Ph.D. in organic chemistry at ETH Zürich. I did a oost-doc in bioinorganic chemistry at the Massachusetts Institute of Technology and a short post-doc in bioorganic chemistry and biophysics at Oxford University.

What are you currently working on?

The development of organelle-targeted redox-active probes, small-molecule fluorophores for super-resolution microscopy, activity-based probes, and fundamental photophysical studies of single molecules.

What do you hope to bring to the journal?

Some expertise in using organic chemistry to develop tools to study cell function and image single-molecules in live cells. Also, some interesting perspectives from a career path that has taken me through several different countries and cultures.

What’s the most interesting challenge in your field at the moment?

Developing multiplexed labeling and imaging methods would allow us to observe multiple different biomolecules with single-molecule resolution. The first step towards spatially-resolved, single-molecule omics!

Sara Sattin, Università degli Studi di Milano

What’s your background?

I studied industrial chemistry and management and then undertook my Ph.D. studies in chemical sciences at the University of Milan, working on glycomimetic antiviral compounds in the framework of anti-adhesive therapies. After some postdoctoral fellowships on supramolecular chemistry (ICIQ, Tarragona, Spain) and chemical biology (University of Oxford, U.K.), in recent years, I have been working on the allosteric modulation of Hsp90, a chaperone protein. I started my research group at the University of Milan in 2017, thanks to an ERC Starting Grant award on eradicating chronic infections.

What are you currently working on?

The focus of the group at the moment is the design and synthesis of small molecular inhibitors of a bacterial protein involved in bacterial persisters formation, a phenotype tolerant to antibiotic treatment that favors the onset of antimicrobial resistance. We are also interested in glycomimetics targeting relevant human and bacterial lectins (i.e., proteins that recognize carbohydrates).

What do you hope to bring to the journal?

I would like to bring the perspective of someone that developed a multifaceted view of the synergic interplay between organic chemistry and chemical biology. I don’t like to put science in tidy labeled boxes, and I think we should try to fully embrace the complexity of the topic we are investigating rather than focusing exclusively on a small part of the picture.

What’s the most interesting challenge in your field at the moment?

There are several interesting challenges to take on in the field, but I think that the most urgent (and interesting) is to give a rapid response to the prevalence of antimicrobial resistance, including the serotype shift observed for some strains after vaccination campaigns. Now, more than ever, this can be achieved effectively only by a strong interplay between chemistry and biology.

Neel Shah, Columbia University

What’s your background?

I received my B.S. in chemistry from New York University. There, I worked with Professor Kent Kirshenbaum on the synthesis and structural characterization of peptidomimetic oligomers. I did my Ph.D. in Professor Tom Muir’s lab, partly at The Rockefeller University and partly at Princeton University. My Ph.D. research involved discovering and characterizing new “ultrafast” split inteins and their application to protein synthesis and engineering. My postdoctoral research was carried out at University of California at Berkeley, in Professor John Kuriyan’s lab. There, I developed new high-throughput methods to examine specificity and allostery in eukaryotic signaling proteins by coupling functional selection assays to deep sequencing of variant libraries.

What are you currently working on?

My lab focuses on phosphotyrosine signaling proteins and pathways. We are developing chemical probes, high-throughput biochemical assays, and cell-based methods to probe allosteric regulation and substrate/ligand specificity in protein tyrosine kinases and protein tyrosine phosphatases. We are particularly interested in phosphotyrosine signaling enzymes that are mutated in human cancers and those that play a direct role in T cell activation.

What do you hope to bring to the journal?

I’m excited to be a part of the Early Career Advisory Board, in large part because I want to push for more opportunities for early-career researchers (not just young principal inversitgators, but trainees also) to showcase their work and get their names out. I’m excited to take on initiatives to have young guest editors, highlight first authors on papers, and maybe even have entire issues with papers/reviews/editorials by early-career researchers!

What’s the most interesting challenge in your field at the moment?

I think the most intriguing challenge in my field is to discover drug allosteric sites in proteins. The signaling enzyme families we study are highly degenerate in their active site structures, making selective inhibition a challenge. Furthermore, given that the proteins we study are cancer-associated, therapeutics that target these enzymes almost always succumb to drug resistance. A major breakthrough in our field would be to develop a systematic way to map “druggable” allosteric sites in proteins and discover potent allosteric inhibitors that bind at that site. A particularly exciting extension of this challenge is the development of allosteric activators of key regulatory signaling enzymes.

Darci Trader, Purdue University

Coming Soon!

Marthe Walvoort, University of Groningen

What’s your background?

I received my Ph.D. in carbohydrate chemistry at the Leiden University under Professor Jeroen Codée, Professor Gijs van der Marel and Professor Hermen Overkleeft. My research included investigating the mechanism of glycosylation of mannuronic acids, and I performed the automated synthesis of β-mannuronic acid alginates and hyaluronan using a solid-phase oligosaccharide synthesizer. Next, I moved to Professor Barbara Imperiali’s lab at Massachusetts Institute of Technology, where I developed inhibitors of phosphoglycosyltransferases inspired by nucleoside antibiotics. Moreover, I established a link between bacterial infection and biomarkers in multiple sclerosis by producing N-linked glycoproteins.

What are you currently working on?

In my independent research group at the Stratingh Institute for Chemistry at the University of Groningen, we combine the power of carbohydrate chemistry and glycobiology to investigate glycans in health and disease. We focus on ‘healthy sugars’ inspired by human milk oligosaccharides and investigate the impact of newly synthesized carbohydrate structures on specific health effects in infants and health-compromised adults.

As bacterial glycoproteins are often involved in pathogenicity, we aim to unravel the mechanisms of bacterial protein glycosylation machinery, focusing on protein glycosyltransferases such as Asn-glucosyltransferase HMW1C (from H. influenza) and Arg-rhamnosyltransferase EarP (from P. aeruginosa). By fully understanding their mechanistic details, we aim to exploit these enzymes as targets for novel antimicrobial design.

What do you hope to bring to the journal?

I am excited to be part of this group of diverse early-career scientists and expect that we will inspire each other to develop new initiatives that will benefit other early-career scientists and the chemical biology society at large. I aim to make ACS Chemical Biology both an attractive platform to show the best chemical biology research, and at the same time, highlight the (team) effort, enthusiasm, and personal stories behind the science through online content.

What’s the most interesting challenge in your field at the moment?

With the increasing amount of knowledge on oligosaccharides’ health effects in developing infants, I look forward to seeing this evolve into novel (medical) food additives, especially for premature and health-compromised infants. The most promising glycan structures will have to be identified and produced on a large scale to achieve this goal. Along the same lines, I think it will be very exciting to see a functional inhibitor of bacterial glycan/glycoprotein synthesis reach the stage where it can be evaluated for antibacterial activity in vivo.

Xiao Wang, Broad Institute

Coming Soon!

Amy Weeks, UW-Madison

What’s your background?

I got my undergraduate degree in chemistry at Massachusetts Institute of Technology, where I performed thesis research investigating the ClpAP proteolytic molecular machine with Dr. Stuart Licht. I went on to earn my Ph.D. at the University of California at Berkeley, in the Department of Chemistry and the Chemical Biology Graduate Program.

As an NSF Graduate Research Fellow in Dr. Michelle Chang’s lab, my research focused on understanding the chemical mechanisms that underpin biological function in Streptomyces cattleya, a soil bacterium that has evolved the unusual ability to biosynthesize organofluorine natural products. After completing my Ph.D., I explored how enzymes can be re-engineered as tools for chemical biology. My research as a Helen Hay Whitney Postdoctoral Fellow in Dr. Jim Wells’s lab at UCSF focused on re-engineering the specificity of the designed peptide ligase subtiligase to enable unbiased capture of free N termini for global sequencing of proteolytic cleavage sites using mass spectrometry-based proteomics. We further developed this technology to capture proteolytic neo-N termini on the surface of live cells, opening up opportunities for mapping proteolysis with subcellular resolution.

What are you currently working on?

My research group develops and applies tools for spatially and temporally resolved mapping of post-translational modifications (PTMs) in living cells. PTMs control the structure, activity, localization, and lifetime of nearly all proteins and are often dysregulated in human disease. However, identifying PTMs has far outpaced assignment of their biological functions, a challenging endeavor that requires detailed information about where and when these modifications occur within the cell. My lab integrates principles from organic chemistry, protein engineering, and mass spectrometry-based proteomics to develop and apply enzymatic tools for spatially and temporally resolved mapping of protein modifications in living cells. These technologies will advance our understanding of how post-translational modifications program biological function, leading to the development of new therapeutic hypotheses to treat human disease.

What do you hope to bring to the journal?

I’m really excited to join the ACS Chemical Biology Early Career Board! I’m hoping to bring an early-career perspective on the most exciting challenges in our field, strengthen connections between emerging researchers in biology and chemistry, and support early career researchers in the chemical biology community.

What’s the most interesting challenge in your field at the moment?

Over the past two decades, chemical tools have enabled us to catalog PTMs to proteins—to ask the ‘who’ (which proteins) and ‘what’ (which PTMs) questions about biological signaling. However, to move beyond simply cataloging these modifications, we need new technologies that will enable us to ask, on a proteome-wide scale, why specific modifications were installed and how they execute their functions on a molecular level. A really exciting challenge is to develop tools that will enable PTM mapping in living cells with spatial and temporal resolution. These tools could provide insights into which modifications have meaningful phenotypic consequences and would allow us to develop a molecular-level understanding of what those consequences are. This information would allow us to functionally prioritize PTMs for follow-up experiments and to dissect previously unappreciated functional nodes in biological signaling pathways. Given the central importance of PTMs in human biology, insights into their spatiotemporal dynamics will advance fundamental biological knowledge and are likely to lead to the identification of new therapeutic targets and biomarkers in human disease.

Kaelyn Wilke, MilleporeSigma

What’s your background?

I’m a Wisconsin native from Green Bay, WI. I received my B.S. in biochemistry from the University of St. Thomas in St. Paul, MN, before starting my chemical biology graduate career in the lab of Professor Erin Carlson at Indiana University in Bloomington, IN. In my doctorate work, I used chemical probes to develop new ways to screen, evaluate, and deactivate histidine kinases, proteins implicated in various bacterial signaling pathways, and promising targets for novel antibacterials. Upon completing my Ph.D., I joined the Chemical Synthesis product management team at MilliporeSigma (formerly Sigma-Aldrich) in Milwaukee, WI. I am currently a Senior Product Manager, leading our chemical biology product roadmap that identifies and commercializes reagents and tools critical to emerging areas of chem-bio and early drug discovery research.

What are you currently working on?

I am currently working on a portfolio that supports research for “undruggables.” While the term “undruggable” can take on slightly different meanings, it generally refers to the 80% of the proteome that has been difficult to target and treat through traditional small-molecule drug discovery. One primary reason is they lack the deep, defined pockets required for inhibitors to bind with high affinity and deactivate them (examples are scaffolding proteins or transcription factors, among others). There is an exciting abundance of global research in this space across academic, pharma, and biotech labs! In my role, I look for ways to translate new developments to the greater drug discovery community by making them accessible to any researcher. For undruggables, I have focused on tools that accelerate lead discovery, target engagement, and targeted protein degradation. This requires an intimate following of the chemical biology space, but it is really just the first step. After a new product (or product area) is identified, I work with a large team to develop and introduce it to the research market.

What do you hope to bring to the journal?

Going from in-lab research to perhaps a less-traditional career route for a Ph.D. chemical biologist, I’ve been challenged to think more broadly about chem-bio research at the interface of academia, pharma, and startups and within the context of an increasingly digitally communicative environment. I hope that I can bring an alternative view to the chem-bio landscape, foster creative ways to make connections between emerging researchers and its readers, and promote the interdisciplinary approaches within chemical biology to address challenging problems in life science.

What’s the most interesting challenge in your field at the moment?

One of the most interesting challenges in looking at the undruggables space is harmonizing data and techniques. As is common in research, one idea seeds many more. If we take protein degraders as an example, these bifunctional and chimeric molecules were developed to eliminate cells’ protein targets by hijacking the cell’s proteasomal system. We’ve observed that since their broader adoption is the development of other bifunctional molecules capable of exploiting several other cellular processes, such as post-translational modifications. How might this growing set of chimeric tools be used holistically? What validation and tools are needed to ensure reproducibility to extract data useful to one researcher’s biological system and be suitable for comparative -omics, computational platforms, and algorithms?

Christina Woo, Harvard University

What’s your background?

I did my graduate training in total synthesis and mechanism of action studies, followed by a postdoctoral fellowship in chemical biology, where I developed a chemical glycoproteomics platform.

What are you currently working on?

We combine the rational design of small molecules and proteins with chemical proteomics to manipulate cellular signals and target “undruggable” proteins.

What do you hope to bring to the journal?

New ideas and new directions!

What’s the most interesting challenge in your field at the moment?

How to determine the function of a small molecule or post-translational modification within a cellular context.

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