Archive for the ‘Collections’ Category

New themed collection on ‘Molecular and nanotheranostics’

A slide summarising the information in this blog post

We’re pleased to announce that a new themed collection from RSC Chemical Biology and RSC Medicinal Chemistry has now been published online.

Read the collection

This themed collection, Guest Edited by Professor Thimmaiah Govindaraju (Jawaharlal Nehru Centre for Advanced Scientific Research, India), covers advancements in molecular and nanotheranostics with particular emphasis on the design of theranostic tools and their selective interaction with biomolecular targets to image and ameliorate pathological conditions. The collection is anticipated to catalyze the development of precision theranostics as advanced and personalizable tools in chemical biology and modern medicine.

The articles in the collection are listed below. Articles in RSC Chemical Biology are open access and free to read.

Editorial

Introduction to the themed collection on ‘Molecular and nanotheranostics’
Thimmaiah Govindaraju
RSC. Chem. Biol., 2024, 5, DOI: 10.1039/D3CB90050A

Reviews

Small molecules and conjugates as theranostic agents
Sumon Pratihar, Krithi K. Bhagavath and Thimmaiah Govindaraju
RSC. Chem. Biol., 2023, 4, 826–849, DOI: 10.1039/D3CB00073G

Recent progress of small-molecule-based theranostic agents in Alzheimer’s disease
Furong Gao, Jiefang Chen, Yuancun Zhou, Letong Cheng, Ming Hu and Xiaohui Wang
RSC. Med. Chem., 2023, 14, 2231–2245, DOI: 10.1039/D3MD00330B

Papers and Communications

Single-chain multicolor-reporter templates for subcellular localization of molecular events in mammalian cells
Sung-Bae Kim, Ramasamy Paulmurugan, Nobuo Kitada and Sojiro A. Maki
RSC. Chem. Biol., 2023, 4, 1043–1049, DOI: 10.1039/D3CB00077J

Fluorescent naphthalimide boronates as theranostics: structural investigations, confocal fluorescence and multiphoton fluorescence lifetime imaging microscopy in living cells
Megan J. Green, Haobo Ge, Stephen E. Flower, Charareh Pourzand, Stanley W. Botchway, Hui-Chen Wang, Navaratnarajah Kuganathan, Gabriele Kociok-Köhn, Meng Li, Suying Xu, Tony D. James and Sofia I. Pascu
RSC. Chem. Biol., 2023, 4, 1082–1095, DOI: 10.1039/D3CB00112A

Cationic Dextrin Nanoparticles for Effective Intracellular Delivery of Cytochrome C in Cancer Therapy
Ankita Sarkar, Sanchita Sarkhel, Deepali Bisht and Amit Jaiswal
RSC. Chem. Biol., 2024, 5, DOI: 10.1039/D3CB00090G

We hope you enjoy this new themed collection from RSC Chemical Biology and RSC Medicinal Chemistry.

Click’n lock: rapid exchange between unsymmetric tetrazines and thiols for reversible, chemoselective functionalisation of biomolecules with on-demand bioorthogonal locking

About this article:

Click reactions play a crucial role in efficiently modifying complex biomolecules, particularly in the realm of biotherapeutics. The continuous challenge lies in their reversible and irreversible transformations, with chemists seeking ultimate control over molecular structures in dilute conditions and crowded environments.

In this groundbreaking article, we introduce the Click’n Lock principle, describing a novel reaction system capable of seamlessly switching from reversible to irreversible click transformations. Termed ‘TeTEx’ for ‘tetrazine – thiol exchange,’ this concept enables on-demand locking of products using bioorthogonal stimuli (dienophiles), providing a transformative switch from reversible to irreversible attachment.

 

Ingo

 

About RSC Chemical Biology

Led by Hiroaki Suga (University of Tokyo), RSC Chemical Biology is dedicated to publishing and disseminating the most exceptionally significant, breakthrough findings of interest to the chemical biology community. All submissions are handled by our experienced and internationally recognised Associate Editors. For more information on the journal, please visit the journal homepage.

As a gold open access journal, there are no barriers to accessing content and your research article will reach an international audience. Please note that the article processing charges are waived until mid-2022, so the journal is currently free to publish in.

RSC Chemical Biology is now indexed in the Directory of Open Access Journals (DOAJ), PubMed Central, Scopus and Web of Science: Emerging Sources Citation Index.  Find out more about the journal and submit your work at rsc.li/rsc-chembio

 

RSC Chemical Biology

Royal Society of Chemistry

www.rsc.org

Predicting small molecule binding pockets on diacylglycerol kinases using chemoproteomics and AlphaFold

About this article

Explore the world of secondary messengers in cell signaling with our latest research on Diacylglycerol (DAG) lipids and their role in cellular communication. DAG kinases (DGK) control cellular DAG levels through phosphorylation, making them crucial in understanding cell signaling pathways. While small molecule inhibitors targeting DGK proteins are valuable tools for investigating DAG signaling, their development has been challenging due to limited information on binding pockets within cells.

Our ground-breaking approach combines chemical proteomics and AlphaFold technology to predict previously undiscovered binding regions for the development of covalent inhibitors.

 

Read the full article here.

 

 

About RSC Chemical Biology

Led by Hiroaki Suga (University of Tokyo), RSC Chemical Biology is dedicated to publishing and disseminating the most exceptionally significant, breakthrough findings of interest to the chemical biology community. All submissions are handled by our experienced and internationally recognised Associate Editors. For more information on the journal, please visit the journal homepage.

As a gold open access journal, there are no barriers to accessing content and your research article will reach an international audience. Please note that the article processing charges are waived until mid-2022, so the journal is currently free to publish in.

RSC Chemical Biology is now indexed in the Directory of Open Access Journals (DOAJ), PubMed Central, Scopus and Web of Science: Emerging Sources Citation Index.  Find out more about the journal and submit your work at rsc.li/rsc-chembio

 

RSC Chemical Biology

Royal Society of Chemistry

www.rsc.org

 

 

The multivalent G-quadruplex (G4)-ligands MultiTASQs allow for versatile click chemistry-based investigations

About this article

G-quadruplexes (or G4s) are four-stranded DNA and RNA structures that fold from guanine (G)-rich sequences. G4 are suspected to play key biological roles in human cells and diseases. Small molecules that selectively target G4s (or G4-ligands) can thus be used as modulators to gain insights into the cell circuitry where G4s are involved. While hundreds of G4-ligands have been designed, synthesized and used, most if not all of them are flat aromatic molecules prone to interact with the duplex-DNA (the major form of DNA within the nucleus), which mechanically decreases their specificity for G4s.

We have developed a brand new molecular design, following a biomimetic approach that hinges on the observation that G4s are stable secondary structures owing to the ability of Gs to self-associate to form G-quartets, and then of G-quartets to self-stack to form the columnar core of G4s. Therefore, using a synthetic G-quartet as a G4-ligand represents a unique example of biomimetic recognition of G4s, relying on a like-likes-like approach, which is the surest pledge for a very high G4-selectivity.

In this article, we report on the design, synthesis and use of synthetic G-quartet-based ligands, also referred to as TASQs (for template-assembled synthetic G-quartets). These TASQs are the latest prototypes of TASQs, being multivalent TASQs (that is why we refer to them as MultiTASQs) able to be functionalized in situ by click chemistry (both CuAAC and SPAAC) for optical imaging and affinity precipitation purposes. These bioorthogonal investigations thus provides unique information about G4 biology.

Click on the infographic to read the full paper!

G-quadruplexes (or G4s) are four-stranded DNA and RNA structures that fold from guanine (G)-rich sequences. G4 are suspected to play key biological roles in human cells and diseases. Small molecules that selectively target G4s (or G4-ligands) can thus be used as modulators to gain insights into the cell circuitry where G4s are involved. While hundreds of G4-ligands have been designed, synthesized and used, most if not all of them are flat aromatic molecules prone to interact with the duplex-DNA (the major form of DNA within the nucleus), which mechanically decreases their specificity for G4s.

 

About RSC Chemical Biology

Led by Hiroaki Suga (University of Tokyo), RSC Chemical Biology is dedicated to publishing and disseminating the most exceptionally significant, breakthrough findings of interest to the chemical biology community. All submissions are handled by our experienced and internationally recognised Associate Editors. For more information on the journal, please visit the journal homepage.

As a gold open access journal, there are no barriers to accessing content and your research article will reach an international audience. Please note that the article processing charges are waived until mid-2022, so the journal is currently free to publish in.

RSC Chemical Biology is now indexed in the Directory of Open Access Journals (DOAJ), PubMed Central, Scopus and Web of Science: Emerging Sources Citation Index.  Find out more about the journal and submit your work at rsc.li/rsc-chembio

 

RSC Chemical Biology

Royal Society of Chemistry

www.rsc.org

 

 

New themed collection on ‘Chemical Proteomics’

A slide summarising the information in this blog post, with images of the two Guest Editors

We’re pleased to announce that a new themed collection from RSC Chemical Biology on Chemical Proteomics has now been published online.

Read the collection

This collection, Guest Edited by Dr Keriann Backus (UCLA, USA) and Dr Stephan Hacker (Leiden University, Netherlands), highlights work on applications of chemoproteomics to study the targets and off-targets of covalent and non-covalent inhibitors, to study the reactivity of amino acids in the proteome, to develop new reactive groups for photocrosslinkers, covalent inhibitors and protein labeling as well as to study post-translational modifications and cofactor binding proteome-wide.

A listing of the articles has been provided below. All articles in RSC Chemical Biology are open access and free to read.

Perspective

Finding a vocation for validation: taking proteomics beyond association and location
Marcus J. C. Long, Jinmin Liu and Yimon Aye
RSC. Chem. Biol., 2023, 3, 110–120, DOI: 10.1039/D2CB00214K

Communications

Quantitative profiling of PTM stoichiometry by resolvable mass tags
Ying Chen, Baiyi Quan, Yuanpei Li, Yuan Liu, Wei Qin and Chu Wang
RSC. Chem. Biol., 2023, 3, 1320–1324, DOI: 10.1039/D2CB00179A

Chemoproteomic mapping of human milk oligosaccharide (HMO) interactions in cells
Abdullah A. Hassan, Jacob M. Wozniak, Zak Vilen, Weichao Li, Appaso Jadhav, Christopher G. Parker and Mia L. Huang
RSC. Chem. Biol., 2023, 3, 1369–1374, DOI: 10.1039/D2CB00176D

Papers

The covalent reactivity of functionalized 5-hydroxy-butyrolactams is the basis for targeting of fatty acid binding protein 5 (FABP5) by the neurotrophic agent MT-21
Esben B. Svenningsen, Rasmus N. Ottosen, Katrine H. Jørgensen, Marija Nisavic, Camilla K. Larsen, Bente K. Hansen, Yong Wang, Kresten Lindorff-Larsen, Thomas Tørring, Stephan M. Hacker, Johan Palmfeldt and Thomas B. Poulsen
RSC. Chem. Biol., 2023, 3, 1216–1229, DOI: 10.1039/D2CB00161F

A peptide-crosslinking approach identifies HSPA8 and PFKL as selective interactors of an actin-derived peptide containing reduced and oxidized methionine
Aaron Maurais and Eranthie Weerapana
RSC. Chem. Biol., 2023, 3, 1282–1289, DOI: 10.1039/D2CB00183G

Chemical proteomic analysis of bile acid-protein targets in Enterococcus faecium
Xinglin Yang, Xiaohui Zhao, Victor Chen and Howard C. Hang
RSC. Chem. Biol., 2023, 3, 1397–1402, DOI: 10.1039/D2CB00178K

Photoreactive bioorthogonal lipid probes and their applications in mammalian biology
Karthik Shanbhag, Kavita Sharma and Siddhesh S. Kamat
RSC. Chem. Biol., 2023, 3, 37–46, DOI: 10.1039/D2CB00174H

Predicting small molecule binding pockets on diacylglycerol kinases using chemoproteomics and AlphaFold
Roberto Mendez, Minhaj Shaikh, Michael C. Lemke, Kun Yuan, Adam H. Libby, Dina L. Bai, Mark M. Ross, Thurl E. Harris and Ku-Lung Hsu
RSC. Chem. Biol., 2023, 3, 422–430, DOI: 10.1039/D3CB00057E

We hope you enjoy this new themed collection from RSC Chemical Biology.

A fluorescent photoaffinity probe for formyl peptide receptor 1 labelling in living cells

About this article

The paper explores developing a chemical tool to label formyl peptide receptor 1 (FPR1) in cells. FPR1 is a sensor in the human innate immune system, which is our body’s ancient first-line response system to detect pathogens. FPR1 is found in our immune cells; it helps these cells move towards sites of infection by sensing peptides released from bacteria.

However, the role of FPR1 is not so simple. FPR1 has been reported in other cells, such as those lining our mucous membranes (gut, lungs etc.), where it presumably comes into contact with many of our friendly bacteria without causing widespread immune activation. This family of proteins (FPRs1-3) can recognise very different molecules, and how this occurs is only beginning to be explored. FPRs can also cause and suppress inflammation and have been linked to numerous diseases (cancer, autoimmune disease). However, it’s unclear how this occurs and how we might modulate it to treat diseases.

In this paper, we designed a tool to label or tag FPR1 with a dye so we can see this sensor on the surface of cells. Our tool also allows us to detect inhibitors that bind FPR1. A key feature of it, is that it permanently labels FPR1. We expect it will be useful to understand the fundamentals of FPR1 biology and explore how we can treat diseases through molecules that activate or repress this protein.

Image of the article

About RSC Chemical Biology

Led by Hiroaki Suga (University of Tokyo), RSC Chemical Biology is dedicated to publishing and disseminating the most exceptionally significant, breakthrough findings of interest to the chemical biology community. All submissions are handled by our experienced and internationally recognised Associate Editors. For more information on the journal, please visit the journal homepage.

As a gold open access journal, there are no barriers to accessing content and your research article will reach an international audience. Please note that the article processing charges are waived until mid-2022, so the journal is currently free to publish in.

RSC Chemical Biology is now indexed in the Directory of Open Access Journals (DOAJ), PubMed Central, Scopus and Web of Science: Emerging Sources Citation Index.  Find out more about the journal and submit your work at rsc.li/rsc-chembio

 

RSC Chemical Biology

Royal Society of Chemistry

www.rsc.org

 

 

SREBP activation contributes to fatty acid accumulations in necroptosis

About this article:

Necroptosis is a type of programmed cell death that is accompanied by extensive inflammatory activity. Previously, it has been shown that lipids accumulate in this process, and the accumulation exacerbates the membrane permeability and cell death in necroptosis.

However, the mechanisms that result in the accumulation of these lipids are unknown.

In this work, the authors used a global transcriptomics approach. They investigated the changes in the expression of proteins involved in lipid biosynthesis and transport to identify upstream mechanisms that cause lipid accumulation in necroptosis. Such a transcriptomics approach combined with further targeted experiments revealed the activation of a key regulatory mechanism of lipid production, namely sterol regulatory element binding proteins.

The authors showed that modulating the activation of sterol regulatory element binding proteins impacts necroptotic phenotype, demonstrating the functional role of these proteins in the accumulation of toxic lipids in necroptosis. Moreover, these results provide insights into mechanisms that regulate lipid production in cell death.

 

Infographic of SREBP activation contributes to fatty acid accumulations in necroptosis

About RSC Chemical Biology

Led by Hiroaki Suga (University of Tokyo), RSC Chemical Biology is dedicated to publishing and disseminating the most exceptionally significant, breakthrough findings of interest to the chemical biology community. All submissions are handled by our experienced and internationally recognised Associate Editors. For more information on the journal, please visit the journal homepage.

As a gold open access journal, there are no barriers to accessing content and your research article will reach an international audience. Please note that the article processing charges are waived until mid-2022, so the journal is currently free to publish in.

RSC Chemical Biology is now indexed in the Directory of Open Access Journals (DOAJ), PubMed Central, Scopus and Web of Science: Emerging Sources Citation Index.  Find out more about the journal and submit your work at rsc.li/rsc-chembio

 

RSC Chemical Biology

Royal Society of Chemistry

www.rsc.org

 

 

A mechanistic study on the cellular uptake, intracellular trafficking, and antisense gene regulation of bottlebrush polymer-conjugated oligonucleotides

A research infographic summarising the linked article.

Read the full article here.

RSC Chemical Biology is now indexed in the Directory of Open Access Journals (DOAJ), PubMed Central, Scopus and Web of Science: Emerging Sources Citation Index.  Find out more about the journal and submit your work at rsc.li/rsc-chembio

RSC Chemical Biology

Royal Society of Chemistry

www.rsc.org

Photoreactive bioorthogonal lipid probes and their applications in mammalian biology

Infographic Bioorthogonal lipid probes: unlocking a world of possibilities by Dr Kamat

 

Read the full article here.

 

 

RSC Chemical Biology is now indexed in the Directory of Open Access Journals (DOAJ), PubMed Central, Scopus and Web of Science: Emerging Sources Citation Index.  Find out more about the journal and submit your work at rsc.li/rsc-chembio

RSC Chemical Biology

Royal Society of Chemistry

www.rsc.org

 

Methyltetrazine as a small live-cell compatible biorthogonal handle for imaging enzyme activities in situ

Infographic about Methyltetrazine as a small live-cell compatible biorthogonal handle for imaging enzyme activities in situ

Read the full article by

 

RSC Chemical Biology is now indexed in the Directory of Open Access Journals (DOAJ), PubMed Central, Scopus and Web of Science: Emerging Sources Citation Index.  Find out more about the journal and submit your work at rsc.li/rsc-chembio

RSC Chemical Biology

Royal Society of Chemistry

www.rsc.org