# Cyclization of Short Peptides Designed from Late Embryogenesis Abundant Protein to Improve Stability and Functionality

## TL;DR

This study shows that cyclizing LEA peptides improves their ability to help E. coli survive drought stress, with some amino acid patterns affecting performance.

## Contribution

The study introduces cyclized LEA peptides and demonstrates their enhanced functionality and stability compared to linear forms.

## Key findings

- Cyclization of LEA peptides significantly improved their drought stress tolerance function in E. coli.
- Peptides with many lysine residues showed reduced performance, possibly due to effects on cyclization efficiency.
- Cyclized LEA peptides have extended potential applications due to improved stability and functionality.

## Abstract

LEA peptides, which are designed based on late embryogenic abundant (LEA) protein sequences, have demonstrated chaperone‐like functions, such as improving drought stress tolerance of Escherichia coli (E. coli). Previous studies have focused on the biological functions of linear LEA peptides. However, the function of cyclic LEA peptide still unknown. This study aimed to explore the cyclic LEA peptides’ bio function like enhance the drought stress tolerance of E. coli by cyclizing the LEA peptide using SICLOPPS (Split Intein Circular Ligation of Peptides and Proteins). The results indicated that cyclization significantly improved the function and extended the potential applications. At the same time, we found that peptides containing numerous lysine residues exhibited reduced performance, which may be due to the exteins’ residues affecting the SICLOPPS efficiency.

Late embryogenic abundant (LEA) peptides are short, disordered peptides that enhance Escherichia coli′s drought stress tolerance. Cyclization of LEA peptides can further improve their properties, such as anti‐desiccation, thereby expanding their potential applications