■ DANIELA BERTINETTI

Image courtesy of Peter Schubart.

Current position: University of Kassel (Germany), Departmentof Biochemistry, postdoctoral fellow with Prof. Friedrich W.Herberg since July 2007 and since 2014 head of the CentralIsotope Laboratory at the University of Kassel.Education: Studied Biochemistry at the Ruhr-Universitat

Bochum (Germany), Diploma in Biochemistry (2003), Advisor:Prof. RolfHeumann; Ph.D. thesis in theDepartment of Biochemistry,University of Kassel, with Prof. Friedrich W. Herberg (2007).Nonscientific interests: Dancing, sewing my own clothes,

geocaching, and traveling.My overall research interests lie in the investigation of

cyclic nucleotide (cNMP)-dependent signaling. Therefore, I aminterested in (i) developing new tools for the in depthcharacterization of cNMP dependent pathways and (ii) analysisof the involvement of these cNMP pathways in various diseasesincluding diabetes mellitus, Parkinson’s disease, Pseudomonasinfections, andmalaria. In our current work, we focus on themaineffector of cAMP in eukaryotic cells: protein kinase A (PKA).PKA is targeted, and therefore spatially and temporally regulated,by A-kinase anchoring proteins (AKAPs). We investigatenovel, cell-permeable peptides, which can disrupt the interactionbetween PKA and AKAPs in an isoform-selective manner. (ReadBertinetti’s article, DOI: 10.1021/cb400900r)

■ BIRGIT HOEGER

Image courtesy of Karolina Pavic.

Current position: European Molecular Biology Laboratory,Heidelberg, Germany, Ph.D. candidate with Dr. Maja Kohn,DOC-Fellowship of the Austrian Academy of Sciences.Education: Graz University of Technology, Austria, M.S. in

Biochemistry, 2012; European Molecular Biology Laboratory,Heidelberg, Germany, research stays 2011 and 2010; Universityof Graz, Austria, B.S. in Chemistry, 2009.Nonscientific interests: Traveling, reading, cooking, hiking,

photography.My research focuses on modulating phosphatase activity by

making use of chemical inhibition and biochemical proteinengineering. Our main proteins of interest are the disease-related phosphatases PRL-3 and PTP1B. For the currentpublication in ACS Chemical Biology, I was involved in a projectwith the aim to develop a selective and cell-active peptideinhibitor of PTP1B that is accessible through commercialsynthesis. Motivated by many elegant approaches publishedrecently, I was happy to take part in the very exciting field ofprobe and tool development. Of high importance, though, is thedevelopment of chemical tools that are readily available and caneasily be accessed by other researchers. Our developed peptidefulfills these requirements and the concept can furthermore beadapted to other enzymes of interest. I look forward to seeingour inhibitor and our strategy being used by the community toanswer further biological questions. (Read Hoeger’s article,DOI: 10.1021/cb400903u)

■ YIJUN HUANG

Image courtesy of Derek Chan.

Current position: Senior Scientist at WuXi AppTec’sPhiladelphia facilityEducation: University of Pittsburgh School of Pharmacy,

Ph.D. in Pharmaceutical Sciences, 2011; Advisor: ProfessorAlexander Domling (Department of Pharmaceutical Sciences).University of Pennsylvania School of Medicine, PostdoctoralResearcher, 2012−2013; Advisor: Professor John D. Lambris(Department of Pathology & Laboratory Medicine).Nonscientific interests: History, badminton, hiking, culture

crossing.

Published: March 21, 2014

Introducing Our Authors

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“I never found it easy,” James W. Black said. Drug discoveryis not even easier today. My research interests span manyaspects of drug discovery, including structure-based drugdesign, synthetic chemistry, structure−activity relationships,assay development, and preclinical drug developmentstrategies. My efforts focus on structure-based discovery ofprotein−protein interaction inhibitors, development of smallmolecules and peptides as novel therapeutics, and bioanalyt-ical assays for pharmacokinetic/pharmacodynamic assess-ment. In the present work, we demonstrate a multidisciplinaryapproach for the discovery of small molecule inhibitors ofp53-Mdm2 interaction via MCR chemistry, pharmacophore-based virtual screening, and structural biology guidedoptimization. This platform opens an avenue for the robustgeneration of drug like compounds to tackle protein−proteininteractions, a challenging class of drug targets. (Read Huang’sarticle, DOI: 10.1021/cb400728e)

■ CHRISTOPH MEYER

Image courtesy of Christoph Meyer.

Current position: Regulatory Affairs Manager, InfectopharmArzneimittel and Consilium GmbH in Heppenheim, Germany.Education: University of Heidelberg, Germany, state

examination in pharmacy, 2006; University of Copenhagen,Denmark, research internship with Prof. Peter Nielsen, 2007;European Molecular Biology Laboratory in Heidelberg,Germany, Ph.D. in Chemical Biology, 2012, Advisor: Dr.Maja Kohn.Nonscientific interests: Mountain sports, music, reading,

cooking.Always intrigued by the special chemical properties and

the diverse biological activities of peptides, I synthesizedand characterized protein tyrosine phosphatase inhibitorsderived from natural substrate sequences in my Ph.D.research. By sequence optimization and specific chemicalmodification I was able to obtain a potent, selective, andcell-permeable inhibitor of the model phosphatase PTP1B.Application of the inhibitor to cells increases the phosphor-ylation level of the insulin receptor, which is a naturalsubstrate of PTP1B proving the activity of the inhibitorinside cells. Hopefully, application of this strategy will leadto the generation of many more selective PTP inhibitors,which are readily accessible to researches around the worldby standard peptide chemistry and can thus help to solveimportant questions in the PTP field. (Read Meyer’s article,DOI: 10.1021/cb400903u)

■ YUTA NIHONGAKI

Image courtesy of Hiroyuki Onodera.

Education: The University of Tokyo, B.A. General Arts andSciences, 2012; The University of Tokyo, Graduate student inGeneral Arts and Sciences, Research Advisor: Prof. MoritoshiSatoNonscientific interests: Rock music, outdoor activity,

cooking.My current research focuses on developing the technologies

for photoactivation of cellular proteins, called optogenetics, todissect complex biological systems based on spatiotemporalcoordination of cellular signaling. The key component ofoptogenetic tools is a natural photoreceptor derived frombacteria, algae, fungus, and plants. We have been conductingprotein engineering studies of photoreceptors, which areessential to build versatile and robust optogenetic tools. In thiswork, we developed photo-inducible homodimerization systemwith improved dimer-forming efficiency, named VVD-52C, bysite-directed mutagenesis of natural fungus photoreceptor, Vivid(VVD). We have demonstrated the competence of VVD-52Cfor making a light-inducible gene expression system more ro-bust and developing photoactivatable caspase-9. We believe thatVVD-52C can provide a versatile system to optically control abroad range of cellular signaling. (Read Nihongaki’s article, DOI:10.1021/cb400836k)

■ GEORGE PRESTON

Image courtesy of Samantha Moore.

Current position: Research Associate, EnvironmentalCarcinogenesis Group, King’s College London, UK.Education: Durham University, UK, B.Sc. in Molecular

Biology and Biochemistry; University of Leeds, UK, M.Sc. in

ACS Chemical Biology Introducing Our Authors

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Chemical Biology; University of Leeds, UK, Ph.D., Supervisor:Prof. Andrew Wilson.Nonscientific interests: Electric guitar, hiking.My research focuses on the chemistry of proteins and pep-

tides. Within this area I am particularly interested in covalentmodifications: their biological occurrence; methods withwhich to identify and quantify them; and the use of syntheticmodifications for probing biological structures and mechanisms.My doctoral studies explored the use of photoaffinity reagentsfor the analysis of disease-related peptide aggregates (amyloid).Over the course of these investigations, it became clear thatamyloid could function as a controlled environment in whichto study photo-cross-linking reactions. In our paper, we use thisapproach to compare three functionalities that are frequentlyemployed within the chemical biology community: trifluor-omethyl aryldiazirine, aryl azide, and benzophenone. We hopethat our findings will help other researchers to get the best out ofthese important tools. (Read Preston’s article, DOI: 10.1021/cb400731s)

■ ALEKSANDRA TWARDA

Imagae courtesy of Aleksandra Twarda.

Current position: Ph.D. student in the laboratory of Prof.Tad A. Holak at the Jagiellonian University in Krakow, Faculty ofChemistry, Cracow, Poland.Education: M.Sc. Eng. at Lodz University of Technology,

Faculty of Biotechnology, Lodz, Poland; partly at the Universityof Boras, Department of Engineering, Sweden, and theUniversity of Turku, Department of Biotechnology, Turku,Finland.Nonscientific interests: Passion for traveling and exploring

different cultures, foreign languages, and art.My Ph.D. research focuses on discovery of small-molecule

inhibitors of the p53-MDM2/X interaction for non-genotoxictherapy of cancer. As described in our manuscript, we haverecently developed potent p53-MDM2 antagonists: compoundYH239 and its prodrug YH239-EE. YH239-EE induces apoptosisin different leukemia cell lines as well as in the patient-derivedacute myeloid leukemia blasts. The observed activity, higher overreference compounds, provides the preclinical basis for furtherstudy of YH239-EE. Moreover, the structures and structure−function relationship of YH239-MDM2, using NMR andX-ray crystallography, should help in the development ofmore efficient drug scaffolds for binding to MDM2/X. Thediscovery of this novel antitumor agent is for me a greatand challenging adventure. (Read Twarda’s article, DOI:10.1021/cb400728e)

■ YUXIAO WANG

Image courtesy of Runqing Diao.

Education: Undergraduate, China Pharmaceutical University,Dr. Jiasheng Tu. Graduate, third year, University of Georgia,Dr. Eileen J. KennedyNonscientific interests: Basketball, tennis, swimming.I am interested in the development of peptides to study kinase

signaling in the cell by perturbing endogenous protein−proteininteractions. This methodology benefits from displacing func-tional kinases instead of direct inhibition. PKA is one of the mostwell-studied kinases and has an established role as globalregulator. However, there is still a huge gap in understanding theeffects of AKAP-mediated localization on PKA signaling. In thispaper, we developed chemically stabilized peptides that can beused in intact cells, making them become powerful investigativetools to study AKAP-localized effects on PKA signaling bydisplacing the R subunit in an isoform-selective manner. I’m gladto be a member of the Department of Pharmaceutical andBiomedical Sciences at UGA and work with Dr. Eileen J.Kennedy. (Read Wang’s article, DOI: 10.1021/cb400900r)

ACS Chemical Biology Introducing Our Authors

dx.doi.org/10.1021/cb500169p | ACS Chem. Biol. 2014, 9, 581−583583