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Olefin Metathesis Polymerization: Overview

Olefin Metathesis Polymerization: Overview

Recently, the development of olefin metathesis polymerization advanced the field of polymer synthesis. Simply put, the reorganization of substituents on their double bonds between two olefins in the presence of a catalyst is known as the olefin metathesis reaction. The use of metathesis reaction for polymer synthesis is called olefin metathesis polymerization.
Ruthenium-based Grubbs catalyst is the most commonly used catalyst for olefin metathesis polymerization. Grubbs catalyst consists of a...

Olefin Metathesis Polymerization: Acyclic Diene Metathesis (ADMET)

Olefin Metathesis Polymerization: Acyclic Diene Metathesis (ADMET)

Acyclic diene metathesis polymerization or ADMET polymerization involves cross-metathesis of terminal dienes, such as 1,8-nonadiene, to give linear unsaturated polymer and ethylene. As ADMET is a reversible process, the formed ethylene gas must be removed from the reaction mixture to complete the polymerization process.
Similar to cross-metathesis, ADMET also involves the formation of metallacyclobutane intermediate by [2+2] cycloaddition of one of the double bonds of a terminal diene with...

Ligand Binding and Linkage

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Protein Modifications in the RER

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Olefin Metathesis Polymerization: Ring-Opening Metathesis Polymerization (ROMP)

Olefin Metathesis Polymerization: Ring-Opening Metathesis Polymerization (ROMP)

Ring-opening metathesis polymerization or ROMP involves strained cycloalkenes as starting materials. The mechanism of ROMP proceeds by reacting cycloalkene with Grubbs catalyst to give metallacyclobutane intermediate which undergoes a ring-opening reaction to form new carbene. The new carbene reacts with another molecule of cycloalkene. Repetition of these steps leads to the formation of an unsaturated open-chain polymer product. All these steps are reversible, however, relieving the ring...

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Updated: Jun 24, 2026

Sequence-specific Labeling of Nucleic Acids and Proteins with Methyltransferases and Cofactor Analogues

Sequence-specific Labeling of Nucleic Acids and Proteins with Methyltransferases and Cofactor Analogues

Published on: November 22, 2014

Olefin metathesis for site-selective protein modification.

Yuya A Lin¹, Justin M Chalker, Benjamin G Davis

¹Department of Chemistry, University of Oxford, UK.

Chembiochem : a European Journal of Chemical Biology

|April 4, 2009

Summary

Olefin metathesis can be adapted for protein modification, offering site-selectivity and efficiency in aqueous conditions. This review details its development and future potential in protein engineering.

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Published on: February 5, 2020

Area of Science:

Biochemistry
Organic Chemistry
Protein Engineering

Background:

Protein modification requires reactions that are site-selective and efficient under mild, aqueous conditions.
Olefin metathesis is a powerful carbon-carbon bond-forming reaction, but its compatibility with proteins needs evaluation.

Purpose of the Study:

To review the development of olefin metathesis for protein modification.
To highlight its applicability in aqueous media and peptidic systems.
To discuss opportunities and challenges in protein engineering for metathesis.

Main Methods:

Review of existing literature on olefin metathesis in peptidic systems.
Analysis of studies demonstrating metathesis in aqueous media.
Discussion of protein engineering strategies for introducing metathesis-compatible amino acids.

Main Results:

Olefin metathesis has been successfully applied to protein substrates.
Development of conditions compatible with biological systems (aqueous, neutral pH, ambient temperature).
Identification of suitable amino acids for genetic incorporation.

Conclusions:

Olefin metathesis is a viable and powerful tool for site-selective protein modification.
Further integration of chemistry and biology is needed to overcome challenges.
Protein engineering holds promise for expanding metathesis applications in bioconjugation.