Archive for the ‘Editor’s Collection’ Category

Editor’s Collection: Lei Liu

The Organic & Biomolecular Chemistry Editor’s collection is a showcase of some of the best articles published in the journal, hand selected by our Associate Editors and Editorial Board members. For this month’s selection, Associate Editor Professor Lei Liu has highlighted some of his favourite recent works. Take a look at what he thought of the articles below, and find out more about the research and the researchers behind the papers in our interviews with the authors.

Lei’s Selection: 

Development of functionalized peptides for efficient inhibition of myostatin by selective photooxygenation



Lei’s comment: “Myostatin, a major negative regulator protein of skeletal muscle growth, has been shown to play a key role in homeostasis of skeletal muscle. To develop new approaches for myostatin-targeting therapy, a series of photooxygenation-functionalized molecules were developed through the conjugation of myostatin-binding peptide and on/off-switchable photooxygenation catalyst. One of these molecules can very efficiently inactivate myostatin through irreversible and catalytic photooxygenation. This study demonstrates a novel strategy for myostatin inhibition.”

Find out more in our interview with the authors

 

Cobalt-catalyzed carbonylation of the C–H bond

Lei’s comment: “The use of cobalt catalysts for C-H activation and functionalization reactions has received increasing attentions in recent years due to two reasons: first, cobalt is a cheap metal; second, cobalt catalysis may provide novel reactivity and selectivity. In the review article the authors surveyed the utility of high-valent cobalt catalysis in C–H carbonylation reactions, showing their applications to many pharmaceutically interesting molecules including benzamides, sulphonamides, benzylamines, aryl anilines, phenols and amino alcohols. The success of cobalt catalysis suggests the need to expand studies in the field, particularly carbonylation of the C(sp3 )–H bond.”

Find out more in our interview with the authors

 

DNAzymes for amine and peptide lysine acylation

Lei’s comment: “Site-selective Lys modification of peptides and proteins at various sequence sites is very important to many biotechnology-related fields. The authors report a very interesting work showing that DNAzymes can be used to catalyze amine acylation, including acylation of a Lys residue in a short DNA-anchored peptide. This study not only expands the scope of DNAzyme catalysis, but also suggests the future possible applicability of DNAzymes for sequence-selective Lys modification of pharmaceutically interesting peptides and proteins.”

Find out more in our interview with the authors

 

Integrating abiotic chemical catalysis and enzymatic catalysis in living cells

Lei’s comment: “Recent experiments have indicated that abiotic catalyst modalities can achieve co-operativity with the enzymatic machinery of living cells. Studies in the direction open doors to two very exciting opportunities: First, “catalysis medicine” where synthetic catalysis is used as a bona fide pharmaceutical modality; second, ‘semi-synthetic life’ that combines the desirable features of living organisms with the unique reactivity of abiotic catalysts. This important review article provides very interesting insights into what need to be done in the coming years, a truly exciting area that would combine the powers of modern chemistry and biology.”

Find out more in our interview with the authors

 

Meet the Editor:

ORCID: http://orcid.org/0000-0001-6290-8602

Professor Lei Liu graduated from University of Science and Technology of China in 1999. He obtained his PhD from Columbia University (2004), and conducted post-doctoral research work at Scripps Research Institute until 2007 when he Liu joined Tsinghua University. Lei Liu works as a Professor in the Chemistry department. His research group is interested in chemical protein synthesis.

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Editor’s Collection: Meet the Authors – Taniguchi, Hayashi et al.

Group photo

From left to right (top row): H Okamoto, Dr A Taniguchi, Dr S Konno (bottom row): Dr A Taguchi, Prof Y Hayashi

Introducing the researchers:

Hideyuki Okamoto obtained his B.S. in pharmacy (2020) from Tokyo University of Pharmacy and Life Sciences. At present, he is a Ph.D. candidate in the graduate school of the university. He is studying the inhibition of bioactive proteins by photooxygenation.

Dr. Atsuhiko Taniguchi obtained his Ph.D. degree at Kyoto Pharmaceutical University, Japan in 2009 under the supervision of Professor Yoshiaki Kiso. He served as a Japan Society for the Promotion of Science (JSPS) research fellow at the same university until 2010. He then worked at Pharmaceuticals and Medical Devises Agency (PMDA) as a reviewer. In 2012, he joined Graduate School of Pharmaceutical Science, The University of Tokyo and Japan Science Technology Agency (JST)-ERATO Kanai Life Science Catalysis Project (Professor Motomu Kanai) as a research fellow. He was appointed as a lecturer at Department of Medicinal Chemistry, Tokyo University of Pharmacy and Life Sciences (Professor Yoshio Hayashi) in 2016, and promoted to an associate professor in 2020. His current research interests include medicinal chemistry and chemical biology in the peptide and protein sciences.

Dr. Sho Konno is an assistant professor of School of Pharmacy at Tokyo University of Pharmacy and Life Sciences (TUPLS) in Japan. He received a B.S. in Pharmacy from TUPLS and a Ph.D. in Pharmacy from Graduate School of Pharmaceutical Sciences, Kyoto University under the supervision of Professor Hideaki Kakeya. After that, he joined the Professor Michael D. Burkart laboratory in Chemistry and Biochemistry at University of California, San Diego as a postdoctoral fellow. He currently develops the coronavirus protease inhibitors. His research also focuses on understanding and utilizing a peptide macrocyclase of natural product biosynthetic enzymes.

Dr. Akihiro Taguchi received his PhD in 2013 from Tokyo University of Pharmacy and Life Sciences under the guidance of Professor Yoshio Hayashi. He worked at Department of Medicinal Chemistry (Professor Yoshio Hayashi Lab.), the Tokyo University of Pharmacy and Life Sciences as an assistant professor in 2013, and promoted to a lecturer in 2020. His current research interests are focused on Peptide Chemistry (development of synthetic methodology for disulfide cyclic peptide) and Medicinal Chemistry.

Prof. Yoshio Hayashi was born in Nagano, Japan, in 1960. After receiving a B.S. at Tokyo University of Pharmacy and an M.S. at Kyoto University, he earned his Ph.D. in 1990 in the Faculty of Pharmaceutical Science, Kyoto University, under the guidance of Emeritus Prof. Haruaki Yajima and Prof. Nobutaka Fujii. His thesis was entitled “Basic research on synthetic peptide vaccines and antiviral agents”. After spending two years at Calpis Food Industry Co., Ltd. and three years at Nippon Steel Corporation (NSC) as a researcher, he was promoted to senior researcher at the Life Science Research Center of the NSC, where he stayed for another eight years. In 1999, he joined Prof. Yoshiaki Kiso’s group in the Dept. of Medicinal Chemistry of Kyoto Pharmaceutical University as a lecturer, and in 2001, was appointed as an associate professor. In 2007, he moved to Tokyo University of Pharmacy and Life Sciences as a full professor. His research interests are peptide chemistry and medicinal chemistry. He created several peptide-and peptidomimetic-based drug candidates such as Plinabulin (Phase III), negamycin derivative, myostatin inhibitory peptide and SARS-CoV 3CL protease inhibitor for the treatment of cancer, genetic disease, muscle disorder and viral infection, respectively. In recognition of his scientific contributions, in 2009, he received the Pharmaceutical Society of Japan Award for Divisional Scientific Promotions.

 

What inspired your research in this area?

There is no effective treatment for muscle atrophic disorders including muscular dystrophy. We would like to provide a new therapeutic strategy based on inactivation of myostatin by photooxygenation.

 

What do you personally feel is the most important outcome of your study?

Our developed functionalized peptides consisting of myostatin-binding peptide and on/off switchable photocatalyst, exert the photooxygenation activity only when binding with myostatin, leading to the target-selective photooxygenation. Due to the irreversible and catalytic photooxygenation, the functionalized peptides produced more than 1500-fold greater inhibitory effect than the original peptide.

 

What directions are you planning to take with your research in future?

We will conduct in vivo study of photooxygenation of myostatin using the functionalized peptides. In addition, the application of this selective photooxygenation can be expand to targets other than myostatin.

 

Read the full article: Development of functionalized peptides for efficient inhibition of myostatin by selective photooxygenation

See the other articles showcased in this month’s Editor’s Collection

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Editor’s Collection: Meet the Authors – Lukasevics and Grigorjeva

Introducing the researchers

Lukass Lukasevics completed his Master’s degree in 2019 at Riga Technical University, Latvia. Currently he is working on his Ph.D. thesis under supervision of Dr. Chem. Liene Grigorjeva at Latvian institute of Organic synthesis, Riga, Latvia. His research interests are focused on the development new methodologies for cobalt catalyzed C-H bond functionalization reactions.

 

 

 

Liene Grigorjeva has received her Ph.D. degree from Riga Technical University (Latvia) in 2013, under the supervision of Prof. Aigars Jirgensons. Then she joined Prof. Daugulis group at the University of Houston (USA) as a postdoctoral researcher (2013-2016). Currently she is principal researcher at Latvian Institute of Organic Synthesis and Assistant Professor at Riga Technical University. Her research interests are focused on the development of novel methodology based on C-H bond functionalization under cobalt catalysis.

 

 

 

What motivates your scientific interest in carbonylation?

Direct carbonylation reactions with CO have been immensely exploited both in academic, as well as industrial chemistry. Research in this area has shown its high potential for the synthesis of compounds with a wide range of utility. We believe that cheap, easy to prepare transition metal catalysts could accelerate the development of new methodology for the synthesis of a high value compounds in medicinal and synthetic organic chemistry.

 

What primary research are you doing in this area?

Our research is focused on the development of novel methodology for C-H functionalization using cobalt catalysis. Interestingly,  cobalt catalysts when compared to noble metals display unique reactivity and selectivity which we are excited to explore and apply towards efficient synthetic methodology targeting structurally diverse compounds.

 

How do you hope this review will help and inspire future research in this area?

C-H functionalization using cobalt catalysis recently has emerged as an attractive alternative to noble metals for their low cost and environmentally friendly properties. With this review we want to highlight the achievements made so far and emphasize that this area is still underdeveloped, thereby promoting researchers to make new developments in this field, hopefully, with industrial applications someday.

 

Read the full article: Cobalt-catalyzed carbonylation of the C–H bond

See the other articles showcased in this month’s Editor’s Collection

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Editor’s Collection: Meet the Author – Christopher Adamson

Christopher Adamson

Can you introduce yourself and tell us a bit about your scientific journey so far?

I grew up on a cattle farm in Alberta. During my undergraduate studies, I developed an appetite for organic chemistry. Professors Todd Lowary and Jeffrey Stryker stand out in my memory. My master’s in organic synthesis was followed by two years in process development at Gilead Sciences. In 2018, I started my Ph.D. studies in Tokyo. I see life as an adventure where the journey matters more than the destination.

What motivates your scientific interest in integrating catalysis?

I am constantly blown away by the beauty and complexity of living systems. Somehow, life has little use for boron, fluorine, or noble metals, in spite of the rich abiotic chemistry of these elements. I am convinced that by incorporating abiotic chemistry within living systems, we can access previously unimaginable chemical transformations and develop new tools for understanding cell biology.

 

What primary research are you doing in this area?

I am working on developing organocatalysis for use within living cells. I hope my work leads to practical methods for installing post-translational modifications and activating prodrugs.

 

How do you hope this review will help and inspire future research in this area?

I aim to draw attention to recent work that sets the current tone. I also want to convince researchers in abiotic catalysis that there are many opportunities in cell biology.

 

Read the full article: Integrating abiotic chemical catalysis and enzymatic catalysis in living cells

See the other articles showcased in this month’s Editor’s Collection

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Editor’s Collection: Meet the Authors – Yao, Przybyla and Silverman

Images of the authors

Left to Right: Yao, Przybyla and Silverman

 

Introducing the researchers:

Tianjiong (Yves) Yao was born in Shanghai, China in 1987. He received his B.S. and Engineer degrees in bioengineering from University of Technology of Compiègne (UTC) in 2012. He received his M.S. degree in molecular and cellular biology at Brandeis University in 2015, where he worked with Lizbeth Hedstrom. He joined the University of Illinois at Urbana-Champaign as a Ph.D. student in biochemistry in 2015. In the laboratory of Prof. Scott K. Silverman he studies DNAzymes, focusing on amine and peptide lysine acylation reactions. Outside of the lab, he is a big fan of horror movies and cannot resist cute kittens.

 

Jack J. Przybyla was born in Baltimore, Maryland, USA in 1997. He received his B.S. degree in biochemistry from Michigan State University in 2019. He joined the University of Illinois at Urbana-Champaign as a Ph.D. student in biochemistry in 2019. In the laboratory of Prof. Scott K. Silverman he studies DNAzymes, focusing on amine and peptide lysine acylation reactions. Outside of the lab, he spends his time writing up outlines for creative projects that he has still yet to finish.

 

Scott K. Silverman was born in Los Angeles, California, USA in 1972. He received his B.S. from UCLA in 1991 working with Christopher Foote on photooxygenation mechanisms and his Ph.D. from Caltech in 1997 working with Dennis Dougherty on high-spin organic polyradicals and molecular neurobiology. After postdoctoral research on RNA folding at University of Colorado Boulder with Thomas Cech, he joined the faculty at University of Illinois at Urbana-Champaign in 2000, where he is Professor of Chemistry. His research group uses in vitro selection to identify DNAzymes with new catalytic activities. Outside of research, he runs, lifts weights, and reads far too much about penguins.

 

What inspired your research in this area?

We are interested in DNAzymes as artificial enzymes identified de novo without needing a natural starting point. In vitro selection from random sequence populations isn’t possible for proteins, so we use nucleic acids, specifically DNA for its favourable practical properties relative to RNA. Amine (lysine) acylation is an important biological regulatory modification, and new amine-acylating DNAzymes could open the door to useful site-specific peptide and protein modification reactions.

 

What do you personally feel is the most interesting outcome of your study?

Showing that DNAzymes have the fundamental capability to catalyze amine acylation with high rate enhancement (we observed up to 1000-fold) is an exciting fundamental advance in catalysis by biologically related molecules.

 

What directions are you planning to take with your research in future?

The longer-term goal of the research in this article is to identify DNAzymes that can site-specifically modify particular lysine residues in folded proteins. This is an ambitious goal, with many challenges that still remain to be addressed. We are excited that we have established the fundamental catalytic capability, and now we have to get this to work with proteins.

 

Read the full article: DNAzymes for amine and peptide lysine acylation

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Editor’s Collection: Kate Jolliffe

The Organic & Biomolecular Chemistry Editor’s collection is a showcase of some of the best articles published in the journal, hand selected by our Associate Editors and Editorial Board members. For this month’s selection, Associate Editor Kate Jolliffe has highlighted some of her favourite recent works. Take a look at what she thought of the articles below, and find out more about the research and the researchers behind the papers in our interviews with the authors.

Kate’s Selection: 

Rational Design of Small Molecule Fluorescent Probes for Biological Applications

Joomyung V. Jun, David M. Chenoweth and E. James Petersson

Kate’s comment: “New fluorophores are highly sought after for the development of tools for biological applications. This review provides a nice overview of the functional fluorescent probes and the factors effecting their photophysical properties. Importantly it provides general guidelines for the rational design of new fluorophores with tailored photophysical properties for applications in chemical biology.”

Find out more in our interview with the authors

 

One-pot synthesis of porphyrin-based [5]rotaxanes

Pablo Martinez-Bulit, Benjamin H. Wilson and Stephen J. Loeb

Kate’s comment: “The synthesis of mechanically interlocked molecules with high degrees of complexity frequently requires multiple synthetic steps, which limits the ability to explore their functionality. Here, Loeb and co-workers report a clever synthesis of porphyrin containing [5]rotaxanes , in a one-pot reaction, opening the door to the synthesis of a wide range of mechanically locked architectures that can be fine-tuned for specific applications.”

Find out more in our interview with the authors

 

Absolute handedness control of oligoamide double helices by chiral oxazolylaniline induction

Ling Yang, Chunmiao Ma, Brice Kauffmann, Dongyao Lia and Quan Gan

Kate’s comment: “The incorporation of a chiral group at the terminus of an aromatic oligoamide strand has been shown to provide complete chiral control in the self-assembly of synthetic antiparallel double helices from quinoline containing foldamers, opening opportunities for the future exploitation of these materials as chiral sensors or catalysts.”

Find out more in our interview with the authors

 

Facile synthesis of sulfotyrosine-containing α-conotoxins

Changpeng Li and Chunmao He

Kate’s comment: “Tyrosine sulfation is an important post-translational modification that is believed to modulate biological function but is underexplored because of difficulties with both the isolation and synthesis of sulphated peptides. Here, He and Li demonstrate the facile synthesis of sulfated conotoxins by combining the sulfate ester deprotection and folding steps into a one pot procedure. Importantly they show that, in the case of conotoxins, the sulfate ester is not as acid labile as expected.”

Find out more in our interview with the authors

 

Meet the Editor:

Katrina (Kate) Jolliffe received her BSc (Hons) in 1993 and PhD in 1997 from the University of New South Wales. She then held positions at Twente University, The Netherlands; the University of Nottingham, UK and the Australian National University before taking up an Australian Research Council QEII fellowship at The University of Sydney in 2002. In 2007 she became a Senior lecturer at the same institution and was promoted to Associate Professor in 2008 and to full Professor in 2009. She currently holds the position of Payne-Scott Professor at The University of Sydney. She is a Fellow of the Australian Academy of Science and has been awarded the Beckwith (2004), Biota (2006), Birch (2017) and H. G. Smith (2018) medals of the Royal Australian Chemical Institute. Her research interests are in the areas of supramolecular, peptide and organic chemistry, with a focus on the design and synthesis of functional molecules, such as molecular sensors capable of detecting anions in biological environments or cyclic peptides for application in biology and medicine.
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Editor’s Collection: Meet the authors – Yang, Ma, Kauffmann, Li and Gan

Introducing the researchers:

Ling Yang was born in 1991 in Qian Jiang, Hu Bei, China. In 2012 she received her bachelor’s degree in Chemical Engineering and Technology from Hubei University. After that, she obtained her Ph.D. degree in January 2018 under the supervision of Prof. Hua Jiang at the Institute of Chemistry, Chinese Academy of Sciences, working toward the synthesis and the characterization of aryl-triazole foldamer receptors to anion recognition. In 2018/2019, she worked as a postdoctoral fellow at Huazhong University of Science and Technology under the guidance of Prof. Quan Gan.

 

 

Chunmiao Ma was born in Hubei, China. She received her bachelor’s degree in chemistry from China University of Geosciences, Wuhan in 2016. She is now working toward a Ph.D. under the supervision of Prof. Quan Gan at Huazhong University of Science & Technology, working on design, synthesis and characterization of artificial foldamers based on aromatic oligoamides.

 

 

Dr. Brice Kauffmann is Crystallographer and head of IECB’s Biophysical and Structural Chemistry core facility. After a PhD in protein crystallography (2003, University of Nancy I), Brice Kauffmann spent three years at the European Molecular Biology Laboratory (EMBL) in Hamburg (Germany) working on the development of a new synchrotron beamline (X12, DESY). He joined the European Institute of Chemistry and Biology in January 2006 as a CNRS Scientist.

 

 

 

Dongyao Li was born in Xiangyang, Hubei, China. In 2015 he received his BS degree in chemistry at Hubei Normal University. He obtained his MS degree from Huazhong University of Science and Technology in 2017 under the supervision of Prof. Gan. and is currently working toward a Ph.D. in the same group, focusing on design, synthesis and applications of artificial foldamers based on aromatic oligoamides.

 

 

Quan Gan was born in 1982 in Wuhan, China. He received bachelor’s degree and master’s degree in Organic Chemistry from Central China Normal University in 2005 and 2008. After that, he took part in a joint doctoral programme under the supervision of Prof. Hua Jiang at the Institute of Chemistry, Chinese Academy of Sciences and Dr. Ivan Huc at the European Institute of Chemistry and Biology, Bordeaux, working toward the synthesis and the characterization of aromatic foldamers to mimic the structures and functions of biomacromolecules, and received his Ph.D. degree in early 2013. In 2013/2014, he worked as a Marie Curie Postdoctoral Research Fellow at the University of Cambridge under the guidance of Prof. Jonathan Nitschke. He has been a Professor working on supramolecular chemistry at the Huazhong University of Science and Technology, China, since December 2014.

 

 

What inspired your research in this area?

The fantastic structures and functions of biomacromolecules always inspire our research.

 

What do you personally feel is the most interesting outcome of your study?

The hybridization of single helices of aromatic foldamers with full handedness control can give rise to the complete chiral control of double helices.

 

What directions are you planning to take with your research in future?

To explore the functions such as chiral sensors or catalysts is the aim that we focus on with foldamers. Here, the complete chiral control of aromatic helices offering a stable chiral environment within the cavity would provide chances to develop these functions, and which is currently being made in our laborotary.

 

Read the full article: Absolute handedness control of oligoamide double helices by chiral oxazolylaniline induction

See the other articles showcased in this month’s Editor’s Collection

See all the full articles on our publishing platform

 

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Editor’s Collection: Meet the author – Pablo Martinez-Bulit

Introducing Dr Pablo Martinez Bulit, first author on “One-pot synthesis of porphyrin-based [5]rotaxanes”

Pablo was born in Mexico City, where he received his B.Sc. in Chemistry from Universidad Nacional Autónoma de México, (UNAM). He obtained his Ph.D. from the University of Windsor, Canada, in 2019, under the supervision of Prof. Stephen Loeb where his research was focused on crystalline materials incorporating rotaxanes and porphyrins. He is currently working as a Postdoctoral Research Associate at the University of Glasgow.

Dr. Pablo Martinez Bulit

 

What inspired your research in this area? 
The long-term focus of this research was to prepare metal-organic frameworks (MOFs) incorporating both a rotaxane linker and a porphyrin linker. We had some initial success and characterised the solvent dependent dynamics of a rotaxane wheel in the solid-state for a porphyrin-based MOF (https://pubs.acs.org/doi/abs/10.1021/acs.cgd.9b00669). However, it remained a challenge to synthesize complex linkers that combined multiple rotaxanes on a porphyrin backbone. This project was a nice challenge as it combined the different research areas of the Loeb Research Group: organic synthesis, supramolecular chemistry to make mechanically interlocked molecules, and crystallography.

 

What do you personally feel is the most interesting outcome of your study? 
The fact that you can make and isolate these molecules this easily still amazes me. As the paper shows, this method is tolerant to a variety of functional groups so the potential to tailor the porphyrin-rotaxane hybrids for different applications is readily achievable.

 

What directions are you planning to take with your research in future?
Upscale the syntheses to make gram quantities and explore their possible incorporation into MOFs. Ideally these types of dynamic rotaxane linkers can be used as mechanically interlocked  switches in the solid-state.

Read the full article: One-pot synthesis of porphyrin-based [5]rotaxanes

See the other articles showcased in this month’s Editor’s Collection

See all the full articles on our publishing platform

 

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Editor’s Collection: Meet the authors – Jun, Chenoweth and Petersson

Left to right: E. James Petersson, Joomyung (Vicky) Jun, and David M. Chenoweth

Let’s meet the researchers!

Joomyung (Vicky) Jun was born in South Korea and received her B.Sc. degree in chemical biology at U. C. Berkeley in 2012, performing undergraduate research with Kenneth Raymond. She then worked with Ronald Zuckermann at the Molecular Foundry in Lawrence Berkeley National Laboratory until 2014. Her research (Ph.D. 2019) at University of Pennsylvania focused on the development of novel and underexplored fluorogenic small molecules. She was co-advised by Professors Chenoweth and Petersson. She is currently a postdoctoral scholar with Ronald T. Raines in the Department of Chemistry at Massachusetts Institute of Technology.

David M. Chenoweth was born in Indiana, USA and received his B.S. degree from Indiana University-Purdue University Indianapolis (IUPUI) in 1999. He worked at Dow AgroSciences and Eli Lilly before joining Peter Dervan’s group at the California Institute of Technology to pursue a Ph.D. After graduation in 2009, he was an NIH Postdoctoral Fellow with Timothy Swager at Massachusetts Institute of Technology. David was appointed Assistant Professor in the Department of Chemistry at the University of Pennsylvania in 2011 and was promoted to Associate Professor with tenure in 2017.  He is also a member of the Biochemistry and Molecular Biophysics Graduate Group in the Perelman School of Medicine and the Bioengineering Graduate Group in the School of Engineering and Applied Science.

E. James Petersson was born in Connecticut, USA and completed his undergraduate education at Dartmouth College and his graduate study under Dennis Dougherty at the California Institute of Technology. After receiving his Ph.D. in 2005, he was an NIH Postdoctoral Fellow at Yale University with Alanna Schepartz. He joined the Department of Chemistry at the University of Pennsylvania in 2008 and the Department of Biochemistry and Molecular Biophysics in the Perelman School of Medicine in 2018. His research has been recognized by several awards, including the Searle Scholar, an NSF CAREER award, and a Sloan Fellowship.

 

What inspires your interest in fluorescent probes?

It is said that “seeing is believing,” and fluorescent probes allow one to directly visualize molecules in complex biological processes, often with high specificity. Small molecule fluorophores enable highly sophisticated microscopy techniques for “seeing” into the body or into cells, techniques that are essential for basic biological research as well as for the diagnosis of diseases, which I find fascinating.

What primary research are you carrying out in the area?

Although numerous fluorescent probes are known, the vast majority of these probes consist of a diminutive set of classical “core” dyes such as coumarin, fluorescein, or BODIPY. Dr. Jun’s thesis research focused on developing underexplored or novel fluorescent cores based on modular scaffolds that exhibited advantages over classic and contemporary dyes.  Prof. Petersson and Prof. Chenoweth have collaborated for many years on various optically active probes, including genetic encoding of fluorescent unnatural amino acids from the Petersson laboratory and photo-convertible small molecules from the Chenoweth laboratory, as well as synergistic projects using tools from the Chenoweth laboratory in protein labeling.

How do you hope this review will help and inspire future research in the area?

One of the challenges in this field is the gap between new probe development and its practical application in a biological system, which are much more complicated than the in vitro system. Says Jun: “I hope this review can be helpful for both chemists and biologists to understand the underlying concept of fluorophore design and to reach a point where chemists can tailor the probe based on the specific biological system of interest.”

 

Read the full article: Rational Design of Small Molecule Fluorescent Probes for Biological Applications

See the other articles showcased in this month’s Editor’s Collection

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Editor’s Collection: Meet the authors – Li and He

Introducing the researchers:

 

 

Chunmao He received his Ph.D. in Bioinorganic Chemistry from the Max Planck Institute for Chemical Energy Conversion (formerly MPI Bioinorganic Chemistry), working on the understanding of the fundamentals in heme protein catalysis, under the direction of Prof. Wolfgang Lubitz. In 2013, he moved to the laboratory of Prof. Jeffrey Bode at ETH Zurich (also ITbM, Nagoya University) to learn peptide synthesis and modification/ligation techniques as a postdoc. Since Aug. 2016, he joined the faculty of the School of Chemistry and Chemical Engineering at the South China University of Technology, as a full Professor. For more information, please read his group page at: http://www2.scut.edu.cn/he/main.htm

 

 

 

 

Changpeng Li obtained his Master degree (2020) from the South China University of Technology in the group of Prof. Chunmao He. His research focused on the development of synthetic strategies for multiple Cys-containing toxins.

 

 

 

 

What inspired your research in this area?

Tyrosine sulfation, an important post-translational modification (PTM), has been shown to present in a number of a-conotoxins (a-CTX). The biological function of this PTM in a-CTX, however, has rarely been studied, mostly because of the lack of a reliable synthetic strategy.

 

What do you personally feel is the most important outcome of your study?

The simple aqueous solution deprotection of the neopentyl protecting group of the sulphate ester, which is used in the standard Fmoc solid phase peptide synthesis, allowed for a one-pot synthetic strategy. Moreover, unlike what’s reported in the literature, the sulphate ester modification here is stable under typical RP-HPLC conditions, i.e. with 0.1% TFA, which greatly simplified our purification and improved the overall yield.

 

What directions are you planning to take with your research in future?

We are using the synthetic strategy developed here for the construction of many other related toxins, and more importantly, we are working on the elucidation of the biological impact of this important PTM on these toxins.

 

Read the full article: Facile synthesis of sulfotyrosine-containing α-conotoxins

See the other articles showcased in this month’s Editor’s Collection

See all the full articles on our publishing platform

 

 

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