These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


Pubmed for Handhelds

PUBMED FOR HANDHELDS

Search MEDLINE/PubMed

  • Title: Expression and purification of an antimicrobial peptide, bovine lactoferricin derivative LfcinB-W10 in Escherichia coli.
    Author: Feng X, Liu C, Guo J, Bi C, Cheng B, Li Z, Shan A, Li Z.
    Journal: Curr Microbiol; 2010 Mar; 60(3):179-84. PubMed ID: 19847484.
    Abstract:
    Antimicrobial peptides (AMPs) are extremely attractive candidate for therapeutic agents due to their wide spectrum of antimicrobial activity and action mechanism different from antibiotics. In this study, a method using genetic engineering for obtaining an antimicrobial peptide, bovine lactoferricin derivative peptide LfcinB-W10, has been developed. According to the coden usage of Escherichia coli, a gene encoding the peptide was synthesized and a recombinant vector of E. coli expression pGEX-EN-LFW was constructed. The LfcinB-W10 peptide fused with glutathione S-transferase (GST) was successfully expressed and about 20 mg fusion protein with 90% purity was obtained from 1 l culture. The recombinant LfcinB-W10 (rLfcinB-W10) was released from fusion protein by the enterokinase digestion, and about the LfcinB-W10 yield reached 300 mug per 1 l culture. The purified rLfcinB-W10 was found to have growth inhibition activity against Staphylococcus aureus (S. aureus) ATCC25923.
    [Abstract] [Full Text] [Related] [New Search]