Introducing Our Authors pubs.acs.org/acschemicalbiology
Cite This: ACS Chem. Biol. 2019, 14, 819−821
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DEBASISH KUMAR GHOSH
ABHISHEK KUMAR
Image courtesy of Debasish Ghosh.
Image courtesy of Abishek Kumar.
Education: 2012, M.S. (Life Sciences), Indian Institute of
Education: 2009, B.Sc. Biotechnology, B.N. College Patna, Patna University, Bihar, India; 2011, M.Sc. Animal Biotechnology, University of Hyderabad, Hyderabad, India Current Position: Ph.D. Student, Computational and Functional Genomics group, Centre for DNA Fingerprinting and Diagnostics, Hyderabad, Telangana, India; Advisor: Dr. Akash Ranjan Nonscientific Interests: Cooking, playing cricket and badminton, learning new languages My graduate study focuses on the understanding of lipid homeostasis in Plasmodium falciparum by the regulatory activity of the acyl-CoA binding proteins (PfACBPs). The objective of the study is to characterize the structural and functional properties of the PfACBPs by several biochemical, cell biological, structural, and computational methods. In this article, I have deciphered the mechanistic details of the differential lipid binding properties of the PfACBPs, other than identifying mefloquine as the small molecule modulator of PfACBPs. I also show how mefloquine binding to PfACBPs competitively inhibits acyl-CoA binding, followed by degradation of the inactive mefloquine-PfACBP complexes by the proteasomal pathway. I also pursue studies on the effect of antimalarial drugs on the human acyl-CoA binding proteins to find the intrinsic toxicity effects of those drugs against human cells. I am involved in another project that seeks to identify the intricate structural features of aggregation-prone proteins by computational studies. (Read Kumar’s article, DOI: 10.1021/ acschembio.9b00003.)
Science Education and Research, Kolkata, India; 2019, Ph.D. (Molecular Neuroscience), Centre for DNA Fingerprinting and Diagnostics, India; Mentor: Dr. Akash Ranjan Current Position: Postdoctoral research associate, Department of Developmental Biology and Neuroscience, University of Cambridge, United Kingdom Nonscientific Interests: Playing cricket, listening to music and audible books, watching documentary films on science fiction, and international politics. My graduate study focuses on multidisciplinary research that aims to explore and understand the mechanism(s) of neurodegenerative disease related protein homeostasis. In brief, my research deals with the studies on proteostasis of aggregationprone proteins. I have identified Huntingtin Interacting Protein K (HYPK) as a global sensor and modulator of different aggregation-prone proteins. HYPK forms unique supramolecular complexes, termed as “H-granules,” that sequester different disease-causing toxic protein aggregates. HYPK is a part of the system’s network of protein degradation pathways. HYPK augments the clearance of poly neddylated protein aggregates through autophagy. I was also involved in several other projects that explored VCP mediated proteostasis, characterization of Plasmodium falciparum acyl-CoA binding proteins, the crystallography of HosA protein, and molecular dynamic simulation studies of SOD1. (Read Ghosh’s article, DOI: 10.1021/ acschembio.9b00003.)
Published: May 17, 2019 © 2019 American Chemical Society
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DOI: 10.1021/acschembio.9b00345 ACS Chem. Biol. 2019, 14, 819−821
ACS Chemical Biology
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Introducing Our Authors
IAN STEPEK
My research focus is the study of protein structures and their conformational dynamics by electron paramagnetic resonance (EPR) spectroscopy. Our technique enables us to determine absolute distance distributions in the nanomolar range between two spin labels that are strategically attached at specific sites within the protein. I am currently developing labeling strategies that rely on the incorporation of noncanonical amino acids into the protein by amber stop codon suppression. In our letter, we present a comparative study of different noncanonical amino acids as targets for site-directed spin labeling via coppercatalyzed azide−alkyne cycloaddition. We investigate their incorporation and labeling efficiency and their spectroscopic properties. (Read Widder’s article, DOI: 10.1021/acschembio.8b01111.)
Image courtesy of Megan Wells
Education: 2013, MChem Chemistry, University of Strathclyde, United Kingdom; Thesis Advisor: Prof. Eva Hevia Current Position: Ph.D. student, Laboratory of Organic Chemistry, ETH Zürich, Switzerland; Advisor: Prof. Jeffrey W. Bod Nonscientific Interests: Seeing the world, playing soccer, making and discovering new music My current research is focused on synthetic fermentation, our platform for the generation of chemical libraries. During my Ph.D. research, I have worked on expanding the synthetic scope of this technique, as well as its application in chemical biology and scientific outreach. This new article details the first use of synthetic fermentation for phenotypic screening, leading to the discovery of an antibacterial peptide with a nanomolar affinity for penicillin-binding proteins. The biocompatibility of synthetic fermentation allows for direct assaying of its product cultures, and its modularity expedites compound resynthesis, SAR studies, and probe development. Using these results as a springboard, we believe that the technique can find broader use in pharmaceutical lead identification and as an educational tool. (Read Stepek’s article, DOI: 10.1021/acschembio.9b00227.)
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MICHAEL GOTSBACHER
Image courtesy of Miguel Castañeda.
Education: 2013, PhD Organic Chemistry, Macquarie University Sydney; 2007, Master of Pharmacy, University of Vienna, Austria Current Position: Research Fellow, School of Medical Sciences (Pharmacology), University of Sydney Nonscientific Interests: Hiking, music, playing pretend with my kids Rather than searching for a ligand suitable for a specific target, we were interested in using an established, druggable ligand to identify its unknown target. Artemisinins, including artesunate, show large potential as drugs beyond their antimalarial activity, but their human protein targets remain elusive. Through an unbiased interrogation of several human cDNA libraries, displayed on a T7 bacteriophage, we identified a human target for artesunatethe pro-apoptotic protein BAD. This not only furthers the understanding of how these fascinating natural products exhibit their diverse bioactivity but might explain the selective anticancer activity described for selected artemisinins. (Read Gotsbacher’s article, DOI: 10.1021/acschembio.8b01004.)
PIA WIDDER
Image courtesy of Michael Dapel.
Education: 2013, B.Sc. in Life Science, University of Konstanz; 2016, M.Sc. in Life Science, University of Konstanz Current Position: Ph.D. researcher at the University of Konstanz in the Department of Chemistry, Advisor: Prof. Malte Drescher Nonscientific Interests: Skiing, tennis, and board games 820
DOI: 10.1021/acschembio.9b00345 ACS Chem. Biol. 2019, 14, 819−821
ACS Chemical Biology
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Introducing Our Authors
HSIEN-WEI (ANDY) YEH
Education: 2008, B.Sc. (hons) Applied Chemistry, National University of Singapore; 2016, Ph.D. Chemistry, University of British Columbia, Supervisor: Stephen G. Withers Current Position: Postdoctoral research fellow, Concordia University, Centre for Applied Synthetic Biology, Supervisor: David Kwan Nonscientific Interests: Traveling, yoga, hiking, watching movies I am interested in understanding the biosynthesis and application of glycoscience. During my graduate research, I studied the interactions of human pancreatic alpha-amylase with its natural substrates, small molecule inactivators and inhibitors. Currently, in my postdoctoral research, I am focused on studying glycotransferases and developing assays for highthroughput screening of inhibitors. In this project, to screen for human fucosyltransferase VI (Fut6) inhibitors, I have developed a strategy utilizing synthetic, fluorogenically labeled oligosaccharides and specific glycosidase enzymes which hydrolyze the specific labeled glycan and result in a fluorescence signal. I have tested a small library of synthetic compounds in a facile highthroughput manner and determined their inhibitory constant around the micromolar range. (Read Zhang’s article, DOI: 10.1021/acschembio.8b01123.)
Image courtesy of Hsien-Wei Yeh.
Education: National Taiwan University, M.S. in Pharmaceutical Science; University of Virginia, Ph.D. in Chemistry (PI: Prof. Hui-wang Ai). Current Position: Department of Chemistry, University of Virginia, Ph.D. student with Dr. Hui-wang Ai (expected to start postdoctoral training with Dr. David Baker at University of Washington in June 2019). Nonscientific Interests: Reading, meditation, movies, learning new things, and spending time with my lovely wife and kids. During my Ph.D. research, I utilized two approaches, synthetic chemistry and protein directed evolution, to expand the capabilities of what natural luciferases can do. I synthesized coelenterazine (marine luciferin) analogs with enhanced water solubility and red-shifted emission and re-engineered luciferases to improve the overall bioluminescence brightness. These newly engineered luciferase−luciferin pairs enable highly sensitive bioluminescence imaging (BLI) and noninvasive tracking of biological events in live animals. Since we have developed luciferase−luciferin pairs that emit photons spanning an appreciable range in the visible spectrum, we are excited at the prospect of performing drug screening by using multicolor bioluminescence assays. Meanwhile, we are enthusiastic about the development of next-generation bioluminescent biosensors on the basis of these newly engineered, ATP-independent bioluminescent reporters. (Read Yeh’s article, DOI: 10.1021/ acschembio.9b00150.)
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XIAOHUA ZHANG
Image courtesy of Xiaohua Zhang.
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DOI: 10.1021/acschembio.9b00345 ACS Chem. Biol. 2019, 14, 819−821
