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Heterologous expression of the novel dimeric antimicrobial peptide LIG in Pichia pastoris.

Authors :
Zhao, Lu
Li, Ling
Hu, Mingyang
Fang, Yuxin
Dong, Na
Shan, Anshan
Source :
Journal of Biotechnology. Feb2024, Vol. 381, p19-26. 8p.
Publication Year :
2024

Abstract

The antimicrobial peptide (AMP) LI is a fusion product of antimicrobial peptide LL37 produced by human neutrophils and Indolicidin secreted by bovine neutrophils. LI retained the antimicrobial activity of the parental peptides and showed high cell selectivity. In this study, the flexible linker Gly-Ser-Gly (G-S-G) was used to ligate LI into dimeric LIG, and constructed the Pichia pastoris (P. pastoris) expression vector pPIC9K-6×His-3×FLAG-LIG. The total protein expression of P. pastoris GS115 reached the highest level (189.6 mg/L) after 96 h induction with 3 % methanol at the initial pH value of 7.0. Finally, 5.9 mg/L of recombinant LIG (rLIG) was obtained after enterokinase digestion and purification. The rLIG had high antimicrobial activity and low hemolytic activity. Compared with monomer LI, GSG linked dimeric LIG, which had no significant change in antimicrobial activity and had good salt ions stability. In this study, the dimeric antimicrobial peptide LIG was successfully expressed, which provided a new idea for the expression of AMPs in the P. pastoris expression system, and had important significance for the application of AMPs. • The flexible linker GSG was used to construct the dimeric antimicrobial peptide LIG. • The antimicrobial peptide LIG was successfully expressed by Pichia pastoris. • The recombinant antimicrobial peptide LIG has high biological activity. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
01681656
Volume :
381
Database :
Academic Search Index
Journal :
Journal of Biotechnology
Publication Type :
Academic Journal
Accession number :
175164558
Full Text :
https://doi.org/10.1016/j.jbiotec.2023.12.015