# Engineering and Exploiting Immobilized Peptide Organocatalysts for Modern Synthesis

## TL;DR

This paper explores how immobilizing peptides as organocatalysts can improve sustainability and efficiency in chemical synthesis.

## Contribution

The paper reviews immobilization strategies for peptides to enhance recycling and catalyst screening in modern synthesis.

## Key findings

- Immobilization methods like covalent binding and adsorption enable easy recovery and reuse of peptide catalysts.
- A variety of supports, including polymers and metal–organic frameworks, have been tested for peptide immobilization.
- Immobilization can accelerate the discovery and application of new peptide catalysts.

## Abstract

Short- and medium-sized peptides have long been used as effective and versatile organocatalysts. In the early 80s, Inoue used diketopiperazines in the Strecker reaction, while Juliá and Colonna reported the epoxidation of chalcone catalyzed by poly-L-Ala. Since then, a variety of peptide-catalyzed reactions have been described. However, peptide synthesis typically implicates the use of toxic reagents and generates wastes; therefore, peptide recycling is expected to significantly improve the overall sustainability of the process. Easy recovery and recycling of peptide catalysts can be expediently attained by covalent binding, inclusion, or adsorption. In addition, immobilization can significantly accelerate the screening of new peptide catalysts. For these reasons, diverse supports have been tested, including natural or synthetic polymers, porous polymeric networks, inorganic porous materials, organic-inorganic hybrid materials, and finally metal–organic frame-works.