Bovine lactoferricin was successfully expressed in E. coli by fusing it with an anionic peptide that neutralized its toxicity to the host bacteria during production — a clever solution to the challenge of making antimicrobial peptides in bacteria.
Key findingLactoferricin B was expressed in E. coli by fusing it with an anionic peptide that neutralized its antibacterial activity during production, allowing
What the researchers found
Lactoferricin B was expressed in E. coli by fusing it with an anionic peptide that neutralized its antibacterial activity during production, allowing the host bacteria to survive while manufacturing the antimicrobial peptide — a practical biotechnology solution.
Why it matters
Relevant for antimicrobial-peptides, peptide-design.
How the study worked
in-vitro study on antimicrobial-peptides, peptide-design.
What this study cannot tell us
See abstract.
How to read the evidence
preliminary evidence.
When this study was published
Published in 2006.
The bigger picture
Advances peptide research.
Questions still open
- Further research needed.
- Clinical translation to evaluate.
Common questions
What was studied?
What was found?
Read the original research
Expression of the cationic antimicrobial peptide lactoferricin fused with the anionic peptide in Escherichia coli.
Applied microbiology and biotechnology, 72(2), 330-8
Citation
Kim, Ha-Kun; Chun, Dae-Sik; Kim, Joon-Sik; Yun, Cheol-Ho; Lee, Ju-Hoon; Hong, Soon-Kwang; Kang, Dae-Kyung. (2006). Expression of the cationic antimicrobial peptide lactoferricin fused with the anionic peptide in Escherichia coli.. Applied microbiology and biotechnology, 72(2), 330-8.