Introducing Our Authors pubs.acs.org/acschemicalbiology
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LISSETTE ANDRES
Education: University of Essex, U.K., School of Biological Sciences, B.Sc. in Molecular Medicine and Biochemistry, 2012, Advisor: Dr. Jody Mason Current Position: Ph.D. graduand, Department of Biology and Biochemistry, University of Bath, U.K., Advisor: Dr. Jody Mason Nonscientific Interests: Traveling and experiencing nature and people in different places, hiking and adventuring, and generally enjoying life My research interests focus on the exploitation and development of library selection systems to isolate novel peptides that can modulate the activities of therapeutically interesting protein targets and chemical modification of these peptides toward valuable therapeutic applications. In our paper, we take a peptide antagonist of oncogenic activator protein-1 (AP-1) isolated by an in cellulo protein-fragment complementation assay (PCA) and successfully truncate it to a more attractive size while maintaining the majority of its binding affinity. This is achieved through the entropic preorganization effects of covalent lactam helix constraints. We further demonstrate that this peptide can be delivered to breast cancer cells where it effectively reduces proliferation. This strategy holds considerable promise for the future development of drugs against AP-1 and other transcription factors less amenable to small molecule modulation. (Read Baxter’s article DOI: 10.1021/acschembio.7b00303.)
Image courtesy of Marco Romero.
Education: B.S. in Chemistry from the University of Puerto Rico, Rió Piedras, 2008, Advisor: Prof. Sandra Peña de Ortiz; Ph.D. in Molecular and Cell Biology from the University of California, Berkeley, 2014, Advisor: Prof. Carolyn R. Bertozzi; Postdoctoral Scholar at the University of California, Berkeley, 2015, Advisor: Prof. Carolyn R. Bertozzi Current Position: Data Privacy Consultant at Focal Point Data Risk, LLC Nonscientific Interests: Architecture, soccer, traveling, languages, and wine tasting In our paper, we investigate the role of intracellular protein O-GlcNAcylation during the development of human neural stem cells. Through the use of chemical inhibitors, we perturb the developmental process of human embryonic stem cells down a neuronal lineage. We demonstrate that the addition of a chemical inhibitor of the O-GlcNAc transferase enzyme causes an acceleration in the generation of human neuronal cells. Our results highlight a manner in which O-GlcNAcylation can affect human embryonic stem cell differentiation and potentially elucidate a mechanism whereby inducing premature neurogenesis and initiating neural growth may be applicable in the study and treatment of neurodegenerative diseases. (Read Andres’s article DOI: 10.1021/acschembio.7b00232.)
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NEIL RUMACHIK
DANIEL BAXTER Image courtesy of Binhong Lin.
Education: B.S. in Chemistry from the University of Wisconsin−Madison (2011, Coon lab); M.S. in Chemistry from the University of California, Berkeley (2016, Bertozzi lab); visiting scholar at Mahidol University in Bangkok, Thailand (2011−2012, Thongboonkerd lab) and the Karolinska Institutet in Stockholm, Sweden (2015−2016, Zubarev lab) Current Position: Chemistry Ph.D. candidate in the Bertozzi lab at Stanford University, expected graduation in early 2018 Nonscientific Interests: Audio engineering, music production, sound design, and traveling Published: August 18, 2017
Image courtesy of Liam Baxter.
© 2017 American Chemical Society
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DOI: 10.1021/acschembio.7b00669 ACS Chem. Biol. 2017, 12, 1963−1964
ACS Chemical Biology
Introducing Our Authors
My graduate research focuses on understanding the regulation and function of protein glycosylation in various biological contexts. More specifically, I am focused on understanding the dynamic mechanisms governing the cycling of O-GlcNAc monosaccharides on and off of intracellular proteins. Aberrant regulation of this modification has been linked to the onset and progression of various diseases, highlighting the need for a more thorough understanding of not only of how the enzymes controlling the cycling of this modification achieve specificity for their thousands of substrates but also the effects of O-GlcNAcylation on protein function. Using a combination of chemical biology and bioanalytical chemistries, we have begun to understand the role that O-GlcNAcylation plays in the differentiation of human embryonic stem cells down a neuronal lineage. Our data establish a novel method to achieve neuronal differentiation much more rapidly than canonical differentiation protocols, and they demonstrate the dramatic effect that perturbations to O-GlcNAcylation can have on developmental biology. (Read Rumachik’s article DOI: 10.1021/acschembio.7b00232.)
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ANDREA STEIGER
Image courtesy of Marissa Burden-Dyke.
Education: B.A. in Chemistry from College of Wooster, 2014, Advisor: Dr. Paul Bonvallet Current Position: Ph.D. candidate and NSF Graduate Research Fellow at the University of Oregon, Department of Chemistry and Biochemistry, Advisor: Dr. Mike Pluth Nonscientific Interests: Running, camping, true crime podcasts, and coffee My research focuses on the development of triggerable COS and H2S donors for research and therapeutic applications. By using caged COS as a source of H2S, we are able to develop H2S donors that are activated only when needed, tune the rate and efficiency of H2S release, and design donors that have improved localization of release. This paper is important in the field because it provides the first evidence that COS-releasing molecules may behave differently than H2S donors. Our findings show that the cytotoxicity profile and mitochondrial bioenergetics of the reported COS donor are unique and significantly different than those observed for other H2S donors, suggesting that COS itself may have unique and underexplored chemical biology. (Read Steiger’s article DOI: 10.1021/acschembio.7b00279.)
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DOI: 10.1021/acschembio.7b00669 ACS Chem. Biol. 2017, 12, 1963−1964
