Category: Front Page
The College of Engineering has honored interdisciplinary scientist, Professor Mark Grinstaff (Chemistry, BME, MSE, MED), with the inaugural Charles DeLisi Award and Distinguished Lecture. Professor Grinstaff will present the Lecture on Thursday, April 2 at 4 p.m. in the Photonics Colloquium Room (PHO 906). In the lecture, “Clinically Informed Biomaterial Design and Engineering,” he will explore how over the past two decades, he and his students have translated ideas from the laboratory into new devices and materials for clinical applications.
The award – established by a generous gift by Professor and Dean Emeritus Charles DeLisi, widely considered the father of the Human Genome Project – is in recognition of Mark Grinstaff’s significant contributions to his field, both as an academic researcher and as an entrepreneur who has co-founded four companies that are translating his ideas into clinical products. In addition to his joint appointments in Chemistry and Biomedical Engineering, Professor Grinstaff directs the Center for Nanoscience and Nanobiotechnology (CNN) and an NIH-funded Translational Research in Biomaterials Training program, and is the inaugural College of Engineering Distinguished Professor of Translational Research and inaugural recipient of the Innovator of the Year Award from BU’s Office of Technology Development. He was also named a College of Engineering Distinguished Faculty Fellow and a Kern Faculty Fellow.
The Grinstaff laboratory, which is currently comprised of more than 20 graduate students and postdoctoral fellows, is funded by the National Institutes of Health, National Science Foundation, The Wallace H. Coulter Foundation, Advanced Energy Consortium, the Center for Integration of Medicine & Innovative Technology, and other agencies. They have advanced several major biomaterials that range from a joint lubricant that could bring longer- lasting relief to millions of osteoarthritis sufferers, to a highly absorbent hydrogel that not only seals wounds, but can later be dissolved and gently removed.
The National Science Foundation’s on line magazine, Science Nation, is featuring a video entitled “Biophotonics poised to make major breakthroughs in medicine.”
Focusing on the Boston University Center for Biophotonic Sensors and Systems (CBSS), the video shows how engineers and scientists collaborate with industry to realize the potential of light waves in the diagnosis and treatment of disease. Among the scientific work highlighted is that of Chemistry professor, Larry Ziegler, and his group who are working with the company, BioTools, to develop a test that uses lasers to diagnose a bacterial infection accurately and quickly.
“Science Nation” is a video series commissioned by the NSF Office of Legislative and Public Affairs. The series is distributed throughout the world, including to LiveScience.com and other media outlets on the Internet, the PBS Newshour Science page, local community TV stations in the U.S. via TelVue Connect Media Exchange, Voice of America for international broadcast distribution, the NSF STEM video portal Science360, the Knowledge Network video stream and Roku channel, and K-12 content distributors in the U.S. and abroad. Some episodes also appear in the nationally-distributed PBS documentary series This American Land.
The National Institutes of Health (NIH) has awarded a 4-year grant to computational chemists, Professor John Straub and his colleague at the University of Maryland (UMD), Professor Devarajan (Dave) Thirumulai, on “Probing the role of membrane and cholesterol on APP‐C99 structure and dynamics.” Protein aggregation in the brain is linked to Alzheimer’s Disease (AD). This neurodegenerative disorder accounts for nearly 50 percent of all cases of senile dementia, is the third leading cause of death in the elderly population, and – devastatingly ‐ is presently incurable. Familial mutations in the Amyloid Precursor Protein (APP), from which the amyloid β (Aβ) protein associated with AD is derived, have been linked with the early onset of amyloid disease.
This computational and theoretical research collaboration between the Straub and Thirumalai groups, augmented by synergistic experimental research collaborations, will explore the structure and dynamics of the 99 amino acid transmembrane fragment of APP (APP‐C99) in membrane environments. This work will have high impact because it has the potential to answer outstanding questions in the field that remain unresolved as a result of conflicting conclusions of experimental studies. By providing novel insights into the dependence of APP structure on familial AD mutations, membrane composition, and interactions with cholesterol, the work will advance the ability to develop preventive or early stage therapeutics for AD.
Professor Sean Elliott, who joined the Department of Chemistry in 2002 and was tenured in 2008, has been promoted to full Professor.
Professor Elliott’s research is at the intersection of biochemical processes and electron-transfer chemistry. By studying how electrons are moved within and between proteins in Biology, he and his group provide a novel, quantitative view of redox regulation, homeostasis, and oxidative stress. Using protein film electrochemisry (PFE), they probe how redox equivalents are stored, manipulated, and transferred in enzymes, in electron-transfer proteins, and in chains of electron-transfer proteins. They have addressed projects that reflect their interests in heme- and ironsulfur cluster-containing electron transfer proteins and enzymes. Professor Elliott has successfully developed new electrochemical methods for addressing questions of enzyme and metalloprotein function to monitor the flow of electrons themselves. Simultaneously, he has a growing research portfolio in the application of Bioinformatics to problems in Metals in Biology. Using sequence similarity network (SSN), he and his group examine the biological diversity of various multi-heme, iron-sulfur cluster and non-heme iron-dependent enzymes and proteins. Further, his group uses PFE and biophysical techniques to investigate the catalytic chemistry of multi-heme enzymes and bacterial peroxidases extensively.
Professor Elliott has received a Scialog Award from the Research Corporation for the Advancement of Science, a Smith Family Young Investigator Award, and the NSF-CAREER Award. In addition to his excellence in research, he has been recognized by Boston University for his educational skills with a Gitner Award for Distinguished Teaching and for advising with the Templeton Award for Student Advising.
A publication from the research group of Professor Adrian Whitty has been selected by the Journal of Biological Chemistry (JBC) as “Paper of the Week.” This distinction is conferred upon JBC papers that the Associate Editors and Editorial Board Members consider to represent the “top 2% of JBC papers in overall importance.” The paper, “Quantitative Analysis of Receptor Tyrosine Kinase-Effector Coupling at Functionally Relevant Stimulus Levels,” provides a rare, quantitative view of how activation of a growth factor receptor is linked to signaling and function. The work is significant because it sheds new light on some of the factors that determine what concentration of growth factor is required to achieve a functional response, and how this functional sensitivity relates to the dose-response behavior observed for receptor activation and for intracellular signaling events. The paper also shows that experiments done using high ligand concentrations can obscure quantitative features of receptor signaling. The journal will publish a profile of the paper’s first author, 5th year graduate student Simin Li (pictured). Other Whitty group investigators who contributed to the work include Dr. Devayani Bhave and Dr. Thomas Riera (former Postdoctoral Fellows), Jennifer Chow and Mariya Atanasova (graduate students), Simone Rauch (undergraduate student), and Dr. Richard Cate (Visiting Scientist).
The high-impact science journal, Nature Chemistry, has published a paper by Professor John A. Porco, Jr., and his colleagues reporting on “Atropselective syntheses of (-) and (+) rugulotrosin A utilizing point-to-axial chirality transfer” (2 February 2015). Rugulotrosin A is a symmetric dimer isolated from an uncharacterised species of Penicillium. The compound displays significant antibacterial activity against a wide range of Gram positive bacteria. Investigating this important compound, the project was conceived by former Porco Group graduate student, Dr. Tian Qin (now a Postdoctoral Associate in the Baran Laboratory at Scripps Research Institute) and Professor Porco. Collaborators for the project included Professor Richard P. Johnson and his colleague Sarah L. Skrabe-Joiner at the University of New Hampshire (Durham, NH) who performed computational studies and Professor Robert J. Capon and Dr. Zeinab Khalil of the Institute of Molecular Bioscience at the University of Queensland (Australia) who carried out natural extract comparisons and biological studies.
Overall, the project team developed a concise, atropselective approach to rugulotrosin A and stereoisomers through point-to-axial chirality transfer which facilitated determination of the absolute configuration of rugulotrosin A. Computational studies modelling the geometry of intermediate diaryl Pd(II) complexes provided a rationale for the atropselectivity observed in the key Suzuki dimerization. Through HPLC analysis of fungal extracts and synthetic samples, it was determined that Penicillium nov. sp. (MST-F8741) generates rugulotrosin A in an atropselective manner. Moreover, the atropisomers and enantiomers of rugulotrosin A were found to have different activities against Gram-positive bacteria, illustrating the importance of stereochemistry on target selectivity.
The cornerstone of organic synthesis is the development of novel chemical methodology that addresses key limitations in efficiency and reactivity. These synthetic methodologies are best demonstrated in the synthesis of biologically relevant molecules such as current drugs and compounds of study. The goal of this 5-year NIH-funded research program being conducted by Professor Scott Schaus and his Group is to develop operationally simple, highly effective methods for constructing building blocks using boron-containing carbon compounds.
The unique properties of boron and the ability to activate organic boronates to deliver carbon nucleophiles has yielded an impressive array of chemical methods and processes. The Schaus Research Laboratory will extend the ability of organoboranes and boronates to deliver carbanion equivalents in novel condensation reactions including chemoselective carbonyl condensations and multicomponent reactions. The reactions will be rendered asymmetric through the development of asymmetric catalysts and chiral boronate reagents and the utility of the methods developed demonstrated by the asymmetric synthesis of pharmaceuticals and natural products. The majority of top selling drugs are sold as a single enantiomer or isomer. The asymmetric construction of pharmaceuticals becomes increasingly more challenging. As it becomes a greater health concern, so will the need for novel methods and chemical substances that prevent and treat human disease.
Mr. Chao Qi is the recipient of the 2015 Vertex Scholar Award. He is a 4th year graduate student in the group of Prof. John A. Porco. Chao was selected based on his demonstrated excellence in organic chemistry. He has developed extremely elegant and enabling synthetic methodology towards two different natural products, making reactions work, and building complex natural product architectures. Highly productive, he has two major publications, with a third manuscript nearing completion. In addition, Chao plays a leadership role in the Porco laboratory and is currently mentoring an undergraduate researcher.
The 2015 award is made possible by Vertex Pharmaceuticals which has provided this generous graduate fellowship in organic chemistry for an exceptional 2nd, 3rd or 4th year graduate student in our Ph.D. program. The BU-Vertex Educational Partnership Program, established in 2010, offers scholarships funded by Vertex Pharmaceuticals, a biotechnology company-based in Cambridge, Massachusetts, US.
The Junior Faculty Fellows program of Boston University’s Rafik B. Hariri Institute for Computing and Computational Science & Engineering was established in 2011 both to recognize outstanding junior faculty at Boston University working in diverse areas of the computational sciences, as well as to provide focal points for supporting broader collaborative research in these areas at BU and beyond. Junior Fellows are selected by the Hariri Institute Executive Steering Committee based on nominations received each spring, and are appointed for a two-year term. Each Fellow will give a Hariri Institute Distinguished Lecture.
Chemistry’s Professor Ksenia Bravaya was named one of the four faculty selected as a Fellow for the 2014-2016 term. Professor Bravaya joined the Department of Chemistry in 2013. Her research focuses on state-of-the-art applications and fundamental studies of the microscopic processes at the heart of bio-imaging of cellular processes and excited state reactions, as well as on the development of new quantum chemical computational methodology aimed at addressing unsolved critical challenges in the simulation of a wide variety of excited electronic state processes in complex systems.
Professor Lawrence Ziegler, Chemistry Department Chair, describes her as “a Theoretical and Computational Chemist of national standing and a rising star in the international community,” adding that “given her strong upward trajectory in highest quality research productivity and her pivotal role in developing University Research initiatives in computational materials science, it is no surprise that she has received this honor to be a Hariri Junior Faculty Fellow. She will be an excellent ambassador for Computational Science.“
The newly configured Center for Molecular Discovery (CMD) builds on the legacy of Boston University’s NIH-funded Center of Excellence, the Center for Chemical Methodology and Library Development (2002-2007 and 2008-2013) to create a new functional core with a focus on the development of small molecule probes and therapeutic leads.
Integrating its small molecule screening collection and medicinal chemistry capabilities with the efforts of high-impact researchers in the biomedical field, the CMD is an enabling core resource for advancing translational science at Boston University.
The CMD will continue to engage in high-throughput screening (HTS) and medicinal chemistry collaborations with external researchers as part of the Chemical Library Consortium (CLC) network formed by the CMLD. The Center has new and ongoing collaborations with several research groups on the BU Charles River Campus, the BU School of Medicine, and the National Emerging Infectious Diseases Laboratories. While some of these collaborations are in early stages, others have progressed to the point of early proposal development, proposal submission, and extramural funding. The CMD has also developed collaborations with companies (e.g., Cubist, AstraZeneca, and Vertex) and scientists at other research universities to further leverage its compound collection.