Related Experiment Video
Updated: Oct 27, 2025
Expression of Recombinant Proteins in the Methylotrophic Yeast Pichia pastoris
Published on: February 25, 2010
Design and heterologous expression of a novel dimeric LL37 variant in Pichia pastoris
Na Zhan1, Licong Zhang1, Hong Yang1
1Institute of Animal Nutrition, Northeast Agricultural University, No. 600 Changjiang Road, Xiangfang District, Harbin, China.
Background:
The antimicrobial peptide LL37 is produced by white blood cells (mainly neutrophils) and various epithelial cells, and has the outstanding advantages of participating in immune regulation, causing chemotaxis of immune cells and promoting wound healing. However, the central domain of LL37 needs to be improved in terms of antimicrobial activity.
Results:
In this study, the amino acid substitution method was used to improve the antimicrobial activity of the LL37 active center, and a dimeric design with a better selection index was selected. A flexible linker was selected and combined with the 6 × His-SUMO tag and LG was successfully expressed using Pichia pastoris as a host. Recombinant LG displayed strong antimicrobial activity by destroying the cell membrane of bacteria but had low hemolytic activity. In addition, compared with monomeric peptide FR, rLG had improved ability to tolerate salt ions.
Conclusion:
This research provides new ideas for the production of modified AMPs in microbial systems and their application in industrial production.
