Application of 6×His-tag in the Expression of Antibacterial Peptide and its Effect on the Antibacterial Activity
Qiang Gong
Abstract
Qiang Gong
Abstract
For the convenience of expression and purification of antimicrobial peptides in vitro,the scorpion defensin gene(sd) and the gene fused with 6×His-tag(sd-His) were reconstructed and expressed in P.pastoris.The two peptides were purified and then the antibacterial activity,thermal and acid stability were detected in vitro.Surprisingly,the antibacterial activity of Sd-His had not been reduced but slightly enhanced.The results indicate that 6 × His-tag can be used for the fusion expression of antimicrobial peptide without affecting its activity.This study provides a simple and efficient method for the expression and purification of antimicrobial peptide.
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For the convenience of expression and purification of antimicrobial peptides in vitro,the scorpion defensin gene(sd) and the gene fused with 6×His-tag(sd-His) were reconstructed and expressed in P.pastoris.The two peptides were purified and then the antibacterial activity,thermal and acid stability were detected in vitro.Surprisingly,the antibacterial activity of Sd-His had not been reduced but slightly enhanced.The results indicate that 6 × His-tag can be used for the fusion expression of antimicrobial peptide without affecting its activity.This study provides a simple and efficient method for the expression and purification of antimicrobial peptide.
Key concepts: Antimicrobial, Peptide, Antibacterial activity, Antibacterial peptide, In vitro, Antimicrobial peptides, Defensin, Chemistry