Wu Yinghan, Ikeno Shinya
Department of Biological Functions Engineering, Kyushu Institute of Technology, Kitakyushu Science and Research Park, Kitakyushu, Fukuoka, Japan.
Chembiochem. 2025 Apr 14;26(8):e202401013. doi: 10.1002/cbic.202401013. Epub 2025 Feb 20.
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.
基于胚胎后期丰富（LEA）蛋白序列设计的LEA肽已显示出类似伴侣蛋白的功能，例如提高大肠杆菌对干旱胁迫的耐受性。先前的研究主要集中在线性LEA肽的生物学功能上。然而，环状LEA肽的功能仍然未知。本研究旨在通过使用肽和蛋白质的分裂内含子环化连接法（SICLOPPS）环化LEA肽来探索环状LEA肽的生物功能，如增强大肠杆菌对干旱胁迫的耐受性。结果表明，环化显著改善了其功能并扩展了潜在应用。同时，我们发现含有大量赖氨酸残基的肽表现出性能下降，这可能是由于外显肽的残基影响了SICLOPPS效率。
