Author Archive

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

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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

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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: Meet the authors – Appel et al.

The Appel Research Group

From left to right: Eric A. Appel, Anton A. A. Smith, Caitlin L. Maikawa and Gillie A. Roth

 

Introducing the researchers:
Eric A. Appel is an Assistant Professor of Materials Science & Engineering at Stanford University. He received a BS in Chemistry (2008) and MS in Polymer Science (2008) from Cal Poly San Luis Obispo, and a PhD in Chemistry (2013) from Cambridge University. His research group at Stanford integrates concepts and approaches from supramolecular chemistry and polymer science to develop (bio)materials that can be used as tools to better understand fundamental biological processes and to engineer advanced healthcare solutions.

Anton A. A. Smith holds a PhD from Aarhus University, Denmark. He will soon be joining the Technical University of Denmark (DTU) where he will be continuing research at the interface of chemistry and biology.

Caitlin L. Maikawa received her BASc (2016) in Chemical Engineering from the University of Toronto. She is currently working on her PhD in Bioengineering at Stanford University with Prof. Eric Appel. Her PhD research focuses on using supramolecular biomaterials to create improved insulin formulations for the treatment of diabetes.

Gillie A. Roth received her B.S. (2015) in Bioengineering from UC San Diego and then completed her PhD in Bioengineering at Stanford University with Eric Appel. Her PhD research focused on designing biomaterials to modulate the pharmacokinetics of therapeutics across diverse disease indications.

 

What inspired your research in this area?
We were already using a conjugate of cucurbit[7]uril with poly(ethylene glycol) (CB[7]-PEG) as a “designer” excipient in insulin formulations (https://www.nature.com/articles/s41551-020-0555-4, https://www.pnas.org/content/113/50/14189.short) to improve insulin stability and alter pharmacokinetics. In this work we figured we could exploit the affinity of CB[7] for the N-terminal phenylalanine on insulin as a tool for insulin modification. Covalent PEG conjugates of insulin had already been examined on numerous occasions in the literature, with insulin bioactivity being heavily dependent on the site of conjugation (steric repulsion from modification in the wrong spot can completely remove activity). Conjugation to the A chain N-terminal glycine significantly reduced activity, making it an interested target for stimulus responsive activation of insulin. Unfortunately, the existing means of selectively functionalizing this site are cumbersome because the preferred site of modification on insulin is the B chain N-terminal phenylalanine. The strong, selective non-covalent binding of CB[7] to this N-terminal phenylalanine presented itself as a practical shortcut to block the nucleophilicity of this site, thereby acting as a non-covalent protecting group, to allow for selective modification of the A-chain N-terminal glycine by simple acylations.

 

What do you personally feel is the most interesting outcome of your study?
For insulin specifically, this work enables a simple approach to selectively functionalize the A chain, which has traditionally been very challenging to modify on account of its poor nucleophilicity compared to the B chain. Our approach shortens the synthetic route towards selective conjugation at this site as the self-assembly provides direct blocking of the site in the reaction flask with simple mixing, but the dynamic non-covalent binding allows for removal of the CB[7] protection directly during purification without need for a deprotection step.

For a broader perspective, non-covalent protection groups in protein and peptide conjugation chemistry are virtually unexplored, and we show that CB-based host-guest complexation provides a simple and effective approach to blocking of aromatic amino acids to drive selective modification elsewhere on the peptide/protein. This approach is potentially applicable to selective conjugation with an array of proteins or peptides.

 

What directions are you planning to take with your research in future?
Insulin conjugates, and possibly stimulus responsive activation, along with excipients in formulation are areas we are very excited about. We imagine there is ample room for developing both the chemistry and clinically relevant translational research using this new approaches to non-covalent protection.

 

Read the full article: Site-selective modification of proteins using cucurbit[7]uril as supramolecular protection for N-terminal aromatic amino acids

 

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Editor’s Collection: Meet the authors – Sperry and Devlin

Rory Devlin (Left) and Jonathan Sperry (Right)

Introducing the researchers:

Rory Devlin received a BSc (Hons) from The University of Auckland in 2017. Currently, he is pursuing his PhD at the same institution under the supervision of Assoc. Prof. Jonathan Sperry, exploring novel biomimetic rearrangements towards the synthesis of alkaloid natural products.

 

Jonathan Sperry completed his Ph.D at the University of Exeter, working on the biomimetic synthesis with Professor Chris Moody. After postdoctoral research with Dame Margaret Brimble FRS at the University of Auckland, he was appointed to a lectureship at the same institution in 2009. Jon was a Royal Society of New Zealand Rutherford Discovery Fellow from 2014-2019.

 

What inspired you to write this review?

Our interest in the nudicaulins was mainly from a synthetic perspective and in particular, validating the unique cascade process in their proposed biosynthesis. We were surprised nobody had written about the nudicaulins before, especially given their fascinating history.

 

What experimental research are you carrying out in the area?

We are using the nudicaulin structure as a lead for drug discovery – the synthetic route to the natural product is very amenable to analogue design. We are also collaborating with Professor Bernd Schneider at the Max Planck Institute for Chemical Ecology to better understand the role and distribution of the nudicaulins.

 

How do you hope this review will inspire future study?

Synthetic chemists’ interest in natural products is generally focused on structure and bioactivity, but this is just the tip of the iceberg – there is so much more to learn and the nudicaulins are a great example. When we choose a natural product for synthesis studies, we now aim to understand why the organism produces the compound which has has led to some great collaborations and research projects I would have never had imagined being involved in a few years ago.

 

Read the full article: The curious yellow colouring matter of the Iceland poppy

 

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Editor’s Collection: Meet the authors – Fascione et al.

From left to right: Robin Brabham, Tessa Keenan and Martin Fascione

Introducing the researchers:

Martin Fascione received his Ph.D. from the University of Leeds in 2009, working with W. Bruce Turnbull on synthetic carbohydrate chemistry. Following a Marie Curie fellowship with Prof. Steve Withers, FRS, in Vancouver and Prof. Gideon Davies, FRS, at the University of York (2012-2014), he took up a lectureship within Chemistry at York in August 2014. His research interests include the chemical glycobiology of rare sugars, synthetic carbohydrate chemistry, and the chemical/enzymatic modification of proteins.

 

Robin Brabham completed his PhD studies in the Fascione group in 2020. His thesis explored the use of amber stop codon suppression as part of new methods for the incorporation of reactive aldehydes into proteins for bioconjugations.

 

Tessa Keenan received her PhD in 2017 from the University of York on protein O-mannosylation. Since completing her PhD, she has undertaken postdoctoral training in the Fascione group in the areas of chemical glycobiology and protein bioconjugation.

 

What inspired your research in this area?

We recently developed an exciting method for modifying proteins (Chem. Sci., 2018, 9, 5585-5593), using reactive a-oxo aldehydes in proteins, but a challenge of this work was extending it to any position within the protein. Periodate oxidation of vicinal diols, or amino alcohols has long been a common method to generate aldehydes in sugar and protein chemistry, it therefore seemed an obvious next step to incorporate such a motif into an unnatural amino acid.

 

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

The ability to incorporate the a-oxo aldehyde internally within proteins is potentially very powerful for future bioconjugation studies. However, the most interesting outcome of the paper is arguably the realisation that the classical unmasking of aldehydes by sodium periodate oxidation is hindered in PBS, a very common buffer for handling proteins.

 

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

Our primary focus is the study sugars at the interface between chemistry and biology, with an emphasis on understanding the roles they play in disease and using this knowledge to develop innovative new therapeutics. To achieve this goal we have been developing new methods for synthesising sugars and modifying proteins using aldehyde handles, and are currently using this toolkit to address unanswered questions in a wide range of diseases, including prostate cancer and leishmaniasis.

 

Read the full article: Rapid sodium periodate cleavage of an unnatural amino acid enables unmasking of a highly reactive α-oxo aldehyde for protein bioconjugation

 

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Editor’s Collection: Meet the authors – Saito and Yagai

Takuho Saito and Shiki Yagai

Introducing the researchers:

Takuho Saito was born in 1996 in Tochigi, Japan. He graduated Chiba University in 2019, and is currently a master’s student under the guidance of Prof. Shiki Yagai at the same University.

Shiki Yagai was born in 1975 in Japan and received his PhD in 2002 at Ritsumeikan University. Then he directly became an assistant professor at Chiba University, and became an associate professor in 2010. In July 2017, he became a full professor in Chiba University. Find out more on his lab webpage.

 

What inspired your research in this area?

We are always inspired by natural molecules and macromolecules to organize into intricate nanostructures, wherein non-covalent interaction such as hydrogen bonds play important role to achieve hierarchical assembly of structures.

 

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

The answer is definitely the fact that just changing the direction of amide groups remarkably improved the thermal stability of our nano-aggregates, as prof. Hackenberger said.

 

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

We are very much interested in the introduction of more amide groups to further improve thermal stability. At the same time, we are interested in the interplay of photoisomerization of azobenzene units and supramolecular chirality.

 

Read the full article: Hierarchical self-assembly of an azobenzene dyad with inverted amide connection into toroidal and tubular nanostructures

 

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Editor’s Collection: Meet the authors – Nielsen, Gothelf and Clo

From left to right: Kurt Gothelf , Emiliano Clo and Thorbjørn Nielsen

 

Introducing the researchers:

Thorbjørn Nielsen: Obtained an MSc. Degree from the Gothelf lab in 2016. He then enrolled in a joint PhD program between Novo Nordisk in Måløv and Aarhus University where he spent half of his time in each place. He graduated in 2020 and is currently a postdoc at the Gothelf lab.

Kurt Gothelf graduated in 1995 from the group of Professor K. A. Jørgensen at Aarhus University. Following a post doctoral stay in Professor M. C. Pirrung’s group at Duke University, USA, he joined the faculty at Aarhus University in 2002 as an Associate Professor. Since 2007 he has been a Full Professor working with bioconjugation, DNA nanotechnology and biosenors. Find out more on his lab webpage.

Emiliano Clo obtained his PhD in Organic Chemistry in 2006 from the Gothelf lab at Aarhus University. He took post doctoral positions from 2007-9 with Prof. Knud Jensen at University of Copenhagen and from 2009-12 in Prof. Henrik Clausen’s Copenhagen Center for Glycomics, spending the last year of which as Research Associate Professor. From 2012, Emiliano works as a Senior Research Scientist at Novo Nordisk’s Research Chemistry Unit.

 

What inspired your research in this area?

Bioconjugation is challenging and both at Novo Nordisk and in the Gothelf group at Aarhus University we follow closely the development of bioconjugation techniques. Itaru Hamachi’s work on directed conjugation strategies has definitely been a steady influence over the years. But, the present study is really an amalgamation of ideas from many sources.

 

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

The most surprising observation was to learn that the conjugation pattern was identical, in spite of the varying the length of the three reagents studied.

 

How do you feel your research has benefitted from collaborating between industry and academia? 

It has been of key importance to the project. Thorbjørn Nielsen (who got his MSc. with Prof. Gothelf) brought the required skillset to Novo Nordisk. Novo Nordisk then provided the materials and equipment required for this project. Together we could pull all the support the projected needed: MS-MS and SPR expertise at Novo Nordisk; cell assays and FACS from Aarhus Unversity. Last, but not the least, Apigenex, Novo’s long-time CRO partners, synthesized the reagents needed.

 

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

Concerning bioconjugation, our future aims are twofold. First, to find reactions that can label proteins quantitatively; second, to devise reagents and protocols that can be applied to more complex proteins or in more complex matrices.

 

Read the full article: disulphide-mediated site-directed modification of proteins

 

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