Bioanalysis Young Investigator Award 2013
2013; Future Science Ltd; Volume: 5; Issue: 13 Linguagem: Inglês
10.4155/bio.13.98
ISSN1757-6199
AutoresAnthony J. O’Donoghue, Serenus Hua, Björn Meyer, Alexandra Ros,
Tópico(s)Health and Medical Research Impacts
ResumoBioanalysisVol. 5, No. 13 News & AnalysisFree AccessBioanalysis Young Investigator Award 2013Anthony J O'Donoghue, Serenus Hua, Björn Meyer & Alexandra RosAnthony J O'DonoghueUniversity of California, 600 16th Street, MC2280, Genentech Hall, San Francisco, CA 94158, USA. , Serenus HuaAsia Glycomics Reference Site, Chungnam National University, Korea, Cancer Research Institute, Chungnam National University, Korea; #436, College of Engineering II, Chungnam National University, 99 Daehak-ro, Yuseong-gu, Daejeon 305-764, Korea. , Björn MeyerMannheim University of Applied Sciences, Institute for Instrumental Analysis and Bioanalysis, Applied Research Center "Biomedical Mass Spectrometry" (ABIMAS), Paul-Wittsack-Str. 10, 68163 Mannheim, Germany. & Alexandra RosDepartment of Chemistry and Biochemistry, Arizona State University, PO Box 871604 Tempe, AZ 85287, USA. Published Online:3 Jul 2013https://doi.org/10.4155/bio.13.98AboutSectionsPDF/EPUB ToolsAdd to favoritesDownload CitationsTrack CitationsPermissionsReprints ShareShare onFacebookTwitterLinkedInRedditEmail Each year, Bioanalysis and Bioanalysis Zone run the Young Investigator Award to identify and reward promising early-career researchers in our community. This year has seen the largest number of nominees yet, with 18 young scientists in the running to win the 2013 Award!We are pleased to announce that this year's Award will again be held in association with Waters and the European Bioanalysis Forum, with the winner receiving US$1000, a year's subscription to Bioanalysis and free open access for their next article published in the journal. They will also receive help with travel costs to ensure they can accept their award in person at the European Bioanalysis Forum Symposium in November, where they will have the chance to make a short presentation on their work.We will be publishing full profiles of all 18 nominees on Bioanalysis Zone (www.bioanalysis-zone.com), and summary profiles will published across four issues of Bioanalysis.Once all the profiles have been published, our Editorial board will help us to narrow the field to five finalists before we open our online vote and ask you to choose our winner.Make sure you don't miss out on the latest news and your chance to vote!Supporting commentsO'Donoghue has developed a technique to simultaneously assay all proteases in a biological sample at exquisitely low concentrations. This global identification of protease specificity allowed him to determine the proteolytic signatures of cancer cells and parasitic organisms, and to subsequently identify the major proteolytic enzymes involved. For industrial applications he is using the method to characterize native or recombinant proteases, and to screen microbial strains for proteases with desirable characteristics. He has recently shown that the technology can also be used for other post-translational modifying enzymes such as kinases and methyl transferases, and the method appears to be amenable to other enzymes as well. The technology was recently published in Nature Methods and the response to the paper has been remarkable. Over 20 new collaborations have recently been established between my laboratory and other investigators from academia and industry, all driven largely by O'Donoghue. O'Donoghue is an exceptional bioanalysis young investigator who is fearless, very motivated, highly capable, creative and exacting. He is also a pleasure to work with and inspirational to all who have the chance to work with him. I highly recommend him with absolutely no reservations for the Bioanalysis Young Investigator Award.Nominated by: Charles S Craik, University of California, 600 16th Street, MC2280, Genentech Hall, San Francisco, CA 94158, USA. charles.craik@ucsf.eduQ Describe the main highlights of your bioanalytical research, & its importance to the bioanalytical community, both now & in the future.The Multiplex Substrate Profiling by Mass Spectrometry (MSP-MS) method has changed the way proteolytic activity in biological samples can be characterized. Previously, activity from individual enzymes was monitored independently. However, cells produce multiple proteases that work in tandem. Therefore, characterization of a single protease does not give a full picture of the functionality. In one application of the method, we have characterized the secreted proteolytic activity of breast cancer cells. The resultant proteolytic signatures are being used for diagnostic and prognostic purposes. In a second application we have determined the proteolytic signature of synovial fluid from rheumatoid arthritis patients. These data will allow us to generate pro-drugs that are specifically activated by proteases in the inflamed joints. Finally, we have determined that extracellular proteolytic activity is altered when the human fungal pathogen Candida albicans grows as a biofilm. Biofilms are typically the reservoir for infection, and until now there was no method to determine the existence of a biofilm in a patient sample. The MSP-MS method is important to the bioanalytical community because it demonstrates that DNA and protein based approaches have limitations to understanding cellular functionality. The MSP-MS method utilizes enzymatic activity to characterize the functional state of biological samples.Q Describe the most difficult challenge you have encountered in the laboratory and how you overcame it?With a background in fungal biology, it was initially a daunting task to develop a MS-based substrate profiling method for proteases. The design and development of this methodology required me to learn peptide chemistry, HPLC and mass spectrometry. However, the most difficult challenge that I encountered during the assay development process was the computational design of the peptide substrates. The goal was to have maximum amino acid sequence diversity in the minimal amount of peptides. This required a complex algorithm, and therefore I collaborated with a mathematician who unfortunately had no knowledge of biochemistry. This required me to teach about basic protein chemistry and learn basic programming. After several failed attempts we succeeded in generating a successful algorithm, which was ultimately used to design each peptide in the MSP-MS assay.Financial & competing interests disclosureThe work was supported by NIH grant P50 GM82250. The authors have no other relevant affiliations or financial involvement with any organization or entity with a financial interest in or financial conflict with the subject matter or materials discussed in the manuscript apart from those disclosed.No writing assistance was utilized in the production of this manuscript.Supporting commentsSerenus is an extremely talented and productive member of my research group. During his brief career, Serenus has already published 15 papers in respected international journals, and has been selected to present his research at numerous conferences and symposia. In the laboratory, he is always busy with another project or manuscript; yet when co-workers need assistance, he is always ready, with a smile. I have known Serenus since his graduate school years, during which we both worked in the same laboratory. Even then, Serenus stood out from other students, not only due to his thorough knowledge of MS and LC methodology, but also because of his undergraduate training at MIT as a chemical engineer, which taught him valuable process optimization and programming skills. Our research inherently generates vast amounts of data, but Serenus has an exceptional ability to quickly spot patterns in the data and distill them into meaningful results. His aptitude for data mining and bioinformatics is essential for today's data-intensive research. Over the years, I have watched Serenus mature from one of my brightest students into an exceptional teacher, leader, and Young Investigator. His combination of solid technical background and sharp, analytical mindset make him, simply, a stellar bioanalytical scientist.Nominated by: Hyun Joo An, Asia Glycomics Reference Site, Chungnam National University, Korea and Cancer Research Institute, Chungnam National University, Korea; #455, College of Engineering II, Chungnam National University, 99 Daehak-ro, Yuseong-gu, Daejeon 305-764, Korea. hjan@cnu.ac.krQ Describe the main highlights of your bioanalytical research, & its importance to the bioanalytical community, both now & in the future.At the Asia Glycomics Reference Site, our research focuses on MS analysis of glycans – complex sugar chains that decorate most human proteins and act as functional components in everything from H1N1 to mother's milk to (according to L'Oreal) anti-aging skin cream. My particular specialty lies in developing and optimizing MS techniques for disease biomarker discovery as well as biotherapeutic protein analysis. I work on essentially all steps of analysis – high-throughput sample preparation, robotic SPE, LC gradient development, MS optimization and data analysis algorithms. While disease biomarkers and biotherapeutic proteins may seem worlds apart, the underlying goal is the same: create a robust, reproducible and technologically accessible method of analysis, which can be easily interpreted and widely disseminated. For biomarkers, we collaborate with clinics and hospitals around the world to identify and characterize glycans that can be used for early detection and/or diagnosis of cancer. For biotherapeutics, we work closely with pharmaceutical companies as well as governmental regulatory agencies to ensure that biopharmaceutical drugs are correctly glycosylated, and satisfy local and international regulatory guidelines.Q Describe the most difficult challenge you have encountered in the laboratory and how you overcame it?In all human relationships, communication is key. Yet, scientists often have notorious difficulties communicating their ideas to the public. Looking back, it was not until I came to Korea that I really learned how to effectively communicate.When I first arrived here, I had a very basic communication problem – as an American working in Korea, I literally did not speak the same language as my students. Of course, they had all studied English in grade school, so we conversed easily about movies, the weather, and other normal, everyday subjects. But, as the conversation turned towards more technical topics, gaps appeared and blank stares increased. As the weeks went by, I found myself changing the way I spoke. I learned to be concise; to quickly drill down to the point; to remove excess flowery language that sounds scientific but does little to convey an idea. In doing so, I not only changed how I taught in the laboratory, but also how I spoke at conferences and how I wrote manuscripts.Through our interactions, my students have taught me to become a better communicator, a better teacher and, ultimately, a better scientist. And for that, I am forever thankful.Financial & competing interests disclosureThe authors have no relevant affiliations or financial involvement with any organization or entity with a financial interest in or financial conflict with the subject matter or materials discussed in the manuscript. This includes employment, consultancies, honoraria, stock ownership or options, expert testimony, grants or patents received or pending, or royalties.No writing assistance was utilized in the production of this manuscript.Supporting commentsI would like to nominate Björn Meyer for the 2013 Bioanalysis Young Investigator Award, because he is an outstanding expert in MALDI-MS with already 19 publications in bioanalytical science. He developed many innovative gel- and LC-based MALDI-MS methods, sometimes by disproving long-held beliefs. Björn uses his in-depth understanding of analytical theory and his very creative mind for method development that he then successfully applies to biological problem solving (e.g., by addressing questions associated with the respiratory chain and setting up proteomic workflows to detect splicing variants and heme modifications). His outstanding versatility as a thinker and a bioanalysis expert is exemplified by his remarkable contributions to diverse fields of biology: bacterial membrane proteome studies, MALDI-MS methods for oligosaccharides, a leukemia project, NMR analysis of a membrane protein and recently published studies on pharmaceutical nanoparticles, and biotyping of mammalian cells. What impresses me the most, however, is Björn's substantial contribution to the MALDI-Imaging and –biotyping capabilities in my laboratory. That is because he is not only a MALDI specialist and team player, but also an excellent supervisor of PhD students.Nominated by: Carsten Hopf, Mannheim University of Applied Sciences, Institute for Instrumental Analysis and Bioanalysis, Paul-Wittsack-Str. 10, 68163 Mannheim, Germany. c.hopf@hs-mannheim.deQ Describe the main highlights of your bioanalytical research, & its importance to the bioanalytical community, both now & in the future.My research in Michael Karas' laboratory at the University of Frankfurt added some new methodical ideas to the field of proteomics.A fundamental challenge is the improvement of workflows for proteins, which are hardly accessible to trypsin proteolysis. As a start, I developed a gel-based MALDI-MS workflow for the analysis of protein complexes containing extremely hydrophobic subunits. Two studies using this technique provided new insights into the composition and functionality of the respiratory chain. Especially the use of less specific cutting enzymes, such as chymotrypsin and elastase, contributed to the required protein sequence coverage to answer the biological problem. The application of such enzymes was afterwards not only studied in detail for the gel- but also the LC-based MALDI-MS approach. I performed several follow-up studies to refine both MALDI-based strategies, that is, I developed a new polyacrylamide gel system and many proteolysis protocols including separation and interpretation strategies for highly complex peptide mixtures.Q How do you envisage the field of bioanalysis evolving in the future?The bioanalysis field will focus more on the qualitative and quantitative analysis of protein isoforms, because only the identification and quantification of the right isoform ensures that the connection to the investigated function in a proteomic study is correct. Therefore, high or 100% sequence coverage is needed to detect preferably all post-translational modifications and splicing variants. A combined application of specific and less specific proteases will support to achieve this aim. The unambiguous peptide identification will be simplified by the permanent improvement in the mass spectrometric field, that is, speed, sensitivity, mass accuracy and resolving power. The mass spectrometric developments, especially in the field of high resolution mass analyzers, will open the door to top-down proteomics for more bioanalysts. The main challenge, however, will be the development of more powerful separation techniques for intact proteins. Another ambition will be to correlate the results of protein species, lipidome and metabolome analysis because only the interaction of all biomolecules can define a biological process in a complete way. In this context, MALDI-Imaging techniques will be used to analyze the spatial distribution of abundant biomolecules.Financial & competing interests disclosureThe authors have no relevant affiliations or financial involvement with any organization or entity with a financial interest in or financial conflict with the subject matter or materials discussed in the manuscript. This includes employment, consultancies, honoraria, stock ownership or options, expert testimony, grants or patents received or pending, or royalties.No writing assistance was utilized in the production of this manuscript.Supporting commentsDr. Ros has been a creative, energetic and insightful young faculty member. The manipulation of single cells and truly unique isolation and concentration strategies for complex mileux of biomolecules contained therein will be a breakthrough for biological and medical studies. She has been able to develop new physics and chemistry on a very fundamental level, and drive those advances intellectually all the way to a final impact on patient care. There are many steps in between her fundamental work and application in the hospital or clinic, but this foundational groundwork must be accomplished first so that the true biochemical information can be unlocked from functioning biological systems. From these core creative ideas, she has been very productive in terms of funding (NIH, NSF CAREER award), establishing a research group (seven students and postdocs), and peer-reviewed publications (nine since arriving at Arizona State University, 33 total).Nominated by: Daniel Buttry, Department Chair, Department of Chemistry and Biochemistry, PO Box 871604, Arizona State University, Tempe, AZ 85287, USA. daniel.buttry@asu.eduQ Describe the main highlights of your bioanalytical research, & its importance to the bioanalytical community, both now & in the future.My research centers on novel bioanalysis techniques evoked by phenomena occuring in nano- and microenvironments that can be exploited for further bioanalytical applications. In contrast to traditional miniaturization techniques down-scaling existing approaches, my research is innovative and unique as it employs nano- and microenvironments to allow for novel migration, separation, conentration, fractionation and analysis techniques. For example, I am among a small group of researchers worldwide exploiting dielectrophoresis for analysis of biomolecules, especially proteins and DNA. Dielectrophoresis has a large potential for bioanalysis, as it can probe intrinsic biomolecular properties based on polarizability influenced by shape, charge, deformation, chemical composition (e.g., nucleotide sequence or amino acid composition). Furthermore, dielectrophoresis has the potential to concentrate biomolecules, thereby improving detection limits, allowing detection in complex samples, with label-free approaches and hyphenation to orthogonal techniques. In my habilitation thesis, I could show for the first time that insulator-based dielectrophoresis can be employed for the separation of DNA in microfluidic systems. My current and future research will focus on the detailed understanding of dielectrophoretic properties of DNA and specifically in investigating protein dielectrophoresis. With this work I will provide the fundamental for the application of dielectrophoresis of biomolecules in the future.Q Where do you see your career in bioanalysis taking you?My career goal is a tenured faculty position with future rank of a full professor. With my research and teaching activities I plan to provide a basis of excellence in novel bionalaytical techniques, educating and mentoring undergraduate and graduate students to succeed in bioanalysis for their furture career in academia and industry. I expect my work having impact in migration techniques and single cell analysis not yet achievable with current approaches. My focus lies on the implementation of tailored nano- and microenvironments to investigate migration mechanisms of biomolecules that are not yet well understood, and for which analytical applications and tools are not yet available. Those include the use of dielectrophoresis and nonintuitive migration mechanisms such as nonequilibrium phenomena. Furthermore, I am interested in single cell analysis techniques coupling microfluidics manipulation of single cells to sample preparation on chip for direct MALDI-MS analysis. I expect to evolve to an expert in these techniques, be recognized in the field of bioanalysis for fundamental studies but also for applications based on those phenomena. As a result of my efforts I expect to contribute to challenging bioanalytical problems including ultra-small sample amounts and mixtures of vast biological complexity.Financial & competing interests disclosureThe authors have no relevant affiliations or financial involvement with any organization or entity with a financial interest in or financial conflict with the subject matter or materials discussed in the manuscript. This includes employment, consultancies, honoraria, stock ownership or options, expert testimony, grants or patents received or pending, or royalties.No writing assistance was utilized in the production of this manuscript.FiguresReferencesRelatedDetails Vol. 5, No. 13 STAY CONNECTED Metrics History Published online 3 July 2013 Published in print July 2013 Information© Future Science LtdPDF download
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