Introducing Our Authors Cite This: ACS Chem. Biol. 2017, 12, 2697-2698
■
PENG-HSUN CHASE CHEN
Education: Seoul National University, B.S. in Chemical and Biological Engineering, 2013; Seoul National University, M.S. in Chemical and Biological Engineering, 2015, Supervisor: Prof. Byung-Gee Kim Current Position: Seoul National University, Ph.D. student in Molecular Biotechnology and Biomaterials, Advisor: Prof. Byung-Gee Kim Nonscientific Interests: Swimming, tennis, gardening, and traveling I am interested in development and optimization of the oxidoreductase system in both enzymology and synthetic biology. During the Master’s course, I was involved in topics related to balancing cofactor usage within a cell and methods to express heterologous oxidoreductases to E. coli in soluble and active form. In my Ph.D. research, I am currently focusing on the development of microbial cell factories involving oxidoreductase for overproducing high-value added compounds. For an effective bioprocess with high conversion, I am working on the removal of unexpected byproducts and ineffective protein expression. In our work, we demonstrated production of (−)-5-hydroxy-equol, a potential antagonist for phytoestrogen, from genistein and showed that a compartmentalized system can enhance the multienzyme system by alleviating the cofactor and protein synthesis burden. (Read Joonwon’s article DOI: 10.1021/acschembio.7b00624.)
Image courtesy of Chi-Yun Wan
Education: National Cheng Kung University, B.Sc. in Chemistry, 2013; National Taiwan University, M.Sc. in Chemistry, 2016, Advisor: Dr. Tsung-Shing Wang Current Position: Texas A&M University, Ph.D. student in Chemistry, Advisor: Prof. Wenshe Liu Nonscientific Interests: Family time, memes, cult movies, and Canidae My research focuses on utilizing siderophores to develop a speciesspecific targeting strategy for bacteria. In this article, we showcase a facile protocol to label a specific genus of bacteria based on vibrioferrin (VF), a siderophore used by vibrios to transport iron. Confirmed by flow cytometry and fluorescence microscopy, the synthesized VF-fluorophore conjugate (VF-FL) can selectively label vibrios, including V. parahemolyticus, V. cholerae, and V. vulnificus, even in the presence of other species such as S. aureus and E. coli. The selective targeting requires both the iron-limiting condition and the siderophore moiety, implying that VF-FL is delivered via VF-related transport machinery. These studies demonstrate that the siderophore scaffold provides access to selective targeting microbes and could be applied to bacterial screening or probing of the microbiota biogeography. (Read PengHsun’s article DOI: 10.1021/acschembio.7b00667.)
■
pubs.acs.org/acschemicalbiology
■
PYUNG-GANG LEE
JOONWON KIM Image courtesy of Bum Seok Park
Education: Seoul National University, B.Sc. Chemical and Biological Engineering, B.Sc. Biological Sciences, 2013 Current Position: Seoul National University, Ph.D. candidate in Chemical and Biological Engineering (expected early graduation, 2019) Advisor: Prof. Byung-Gee Kim Nonscientific interests: Playing table tennis, soccer, cooking, and watching movies My Ph.D. research topic is to develop efficient whole-cell biocatalytic systems to prepare novel and functional polyphenol derivatives. To maximize the catalytic capacity of whole cells, a compartmentalized expression strategy, or usage of biocompatible Published: November 17, 2017
Image courtesy of Minwoo Kim
© 2017 American Chemical Society
2697
DOI: 10.1021/acschembio.7b00955 ACS Chem. Biol. 2017, 12, 2697−2698
ACS Chemical Biology
■
additives to increase substrate-product solubility, is utilized. In addition, mining novel enzymes and semirational enzyme engineering to enhance their stereoselectivity or catalytic activity are also included in my research area. Our paper in ACS Chemical Biology introduces an efficient strategy to prepare two novel isoflavone derivatives, 5-hydroxy-equol and 5-hydroxy-dehydroequol, using a simple whole cell biocatalyst. Whole-cell biocatalytic systems with proper genetic manipulation offer massive preparation of the compounds with fine purity. Therefore, this study opens up a powerful research opportunity to get novel bioactive isoflavone derivatives, which could be studied further for some positive effects to human health. (Read Lee’s article DOI: 10.1021/acschembio.7b00624.)
■
Introducing Our Authors
SHABNAM SHARIFZADEH
Image courtesy of Gita Kiaei
DYLAN RIGGS
Education: Tehran University of Medical Sciences, Department of Pharmacy, Pharm. D., 2013; University of Minnesota, Department of Chemistry, M.S., 2016 Current Position: University of Minnesota, Department of Chemistry, Ph.D. candidate in Chemistry, Advisor: Prof. Erin Carlson Nonscientific Interests: Traveling, yoga, hiking, cooking, reading My Ph.D. research is focused on studying the bacterial cell wall and the enzymes involved, with a high emphasis on penicillinbinding proteins (PBPs). PBPs have received much attention for many decades as crucial antibacterial targets and for their role in antibiotic resistance. However, the specific roles of individual family members in each bacterial strain are yet to be understood. In my research group, we firmly believe that with the alarming rate of antibiotic resistance, it is critical to gain a better understanding of known targets. We are interested in developing PBP-selective chemical probes and using them to track individual PBPs in live cells through activity-based protein profiling (ABPP). In this paper, development of a comparatively simple β-lactone scaffold and its specificity for PBPs is presented. Through slight structural modifications to the probe, we could selectively target PBP2x and -2b in Streptococcus pneumoniae and map their activity throughout the cell cycle for the first time. We are working on the expansion of this approach to other microorganisms and related enzymes. (Read Shabnam’s article DOI: 10.1021/ acschembio.7b00614.)
Image courtesy of Andrew Green
Education: California State University, Channel Islands, B.S. in Chemistry, Research Advisor: Prof. Blake Gillespie; University of California, Riverside, M.S. in Biochemistry and Molecular Biology, 2015 Current Position: University of California, Riverside, Ph.D. Candidate in Biochemistry and Molecular Biology, Research Advisor: Prof. Ryan R. Julian Nonscientific Interests: Hiking, gardening, playing sports, and cooking I am interested in understanding biological aging and protein damage. One primary focus is the spontaneous deamidation of asparagine, which yields four isomers of aspartic acid. This modification is known to have detrimental impacts in the cell and reduces the efficacy of protein drugs. Although deamidation is a pervasive post-translational modification, it remains difficult to characterize due to the chemical similarity of the four isomeric degradation products. To address this, we have employed photodissociation and radical chemistry within a mass spectrometer to identify and quantify peptide isomers based on fragmentation patterns. By developing a method to analyze all four isomers, we have been able to gain insight into factors that influence the deamidation outcomes. This information offers the potential to better understand age-related decay and should be an important consideration for designing and developing protein therapeutics. (Read Dylan’s article DOI: 10.1021/acschembio.7b00686.) 2698
DOI: 10.1021/acschembio.7b00955 ACS Chem. Biol. 2017, 12, 2697−2698
