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Themed collection Methodology development for protein modifications

8 items
Review Article

Chemical methods for modification of proteins

The field of protein bioconjugation draws attention from stakeholders in chemistry, biology, and medicine. This review provides an overview of the present status, challenges, and opportunities for organic chemists.

Graphical abstract: Chemical methods for modification of proteins
Communication

Red-shifted backbone N–H photocaging agents

A 3-nitrodibenzofuran cure provides blue-shifted reactivity in vinylogous photocleavage processes.

Graphical abstract: Red-shifted backbone N–H photocaging agents
Open Access Communication

Efficient and selective antibody modification with functionalised divinyltriazines

We have developed a highly efficient disulfide rebridging strategy for the modification of antibodies with substituted divinyltriazine linkers.

Graphical abstract: Efficient and selective antibody modification with functionalised divinyltriazines
From the themed collection: Chemical biology in OBC
Communication

Disulphide-mediated site-directed modification of proteins

Site-directed addition of a single thiols handle to proteins by means of temporary disulphide rebridging of solvent exposed disulphides is obtained with a new labelling reagent.

Graphical abstract: Disulphide-mediated site-directed modification of proteins
From the themed collection: Chemical biology in OBC
Communication

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

Supramolecular protection of N-terminal aromatic amino acids through complexation with cucurbit[7]uril can enable site-selective protein modification of unfavored motifs.

Graphical abstract: Site-selective modification of proteins using cucurbit[7]uril as supramolecular protection for N-terminal aromatic amino acids
From the themed collection: Editor’s Collection
Open Access Communication

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

A genetically incorporated ThrK unnatural amino acid can undergo rapid periodate oxidation to reveal a reactive internal α-oxo aldehyde.

Graphical abstract: Rapid sodium periodate cleavage of an unnatural amino acid enables unmasking of a highly reactive α-oxo aldehyde for protein bioconjugation
From the themed collection: Chemical biology in OBC
Communication

A laccase-catalysed tyrosine click reaction

The tyrosine click reaction of peptides/proteins with the tyrosine modification reagent, N-methyl luminol, was catalysed by a laccase in the presence of molecular oxygen (O2) at 37 °C.

Graphical abstract: A laccase-catalysed tyrosine click reaction
From the themed collection: Chemical biology in OBC
Paper

Selective modification of sulfamidate-containing peptides

Hybrid peptides whose N-terminal residues are activated in the form of α-methylisoserine cyclic sulfamidates exhibit rich reactivity as electrophiles, allowing site- and stereoselective modifications at different backbone and side chain positions.

Graphical abstract: Selective modification of sulfamidate-containing peptides
8 items

About this collection

The chemical modification of proteins is an important and ever growing field. This collection, guest edited by Professors Annemieke Madder (Ghent University, Belgium), Gonçalo Bernardes (University of Cambridge, UK), and Hiroyuki Nakamura (Tokyo institute of Technology, Japan) showcases the latest advances in Methodology Development for Protein Modifications. The collection scope covers but is not limited to all aspects of new synthetic methods towards protein modification and their application.
 
New articles will be added to the collection upon publication. Please return to this page frequently to see the collection grow.

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