Archive for December, 2020

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.

Digg This
Reddit This
Stumble Now!
Share on Facebook
Bookmark this on Delicious
Share on LinkedIn
Bookmark this on Technorati
Post on Twitter
Google Buzz (aka. Google Reader)

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

See all the full articles on our publishing platform

Digg This
Reddit This
Stumble Now!
Share on Facebook
Bookmark this on Delicious
Share on LinkedIn
Bookmark this on Technorati
Post on Twitter
Google Buzz (aka. Google Reader)

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

See all the full articles on our publishing platform

Digg This
Reddit This
Stumble Now!
Share on Facebook
Bookmark this on Delicious
Share on LinkedIn
Bookmark this on Technorati
Post on Twitter
Google Buzz (aka. Google Reader)

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

See all the full articles on our publishing platform

Digg This
Reddit This
Stumble Now!
Share on Facebook
Bookmark this on Delicious
Share on LinkedIn
Bookmark this on Technorati
Post on Twitter
Google Buzz (aka. Google Reader)

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

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

See all the full articles on our publishing platform

Digg This
Reddit This
Stumble Now!
Share on Facebook
Bookmark this on Delicious
Share on LinkedIn
Bookmark this on Technorati
Post on Twitter
Google Buzz (aka. Google Reader)