Multimerized bovine lactoferricin derivative was expressed as a fusion protein in E. coli, with multiple copies per fusion increasing yield — scaling up antimicrobial peptide production for practical applications.
Key findingMultimerized fusion expression of lactoferricin derivative LfcinB15-W4,10 in E. coli achieved increased recombinant peptide yield through multiple tan
What the researchers found
Multimerized fusion expression of lactoferricin derivative LfcinB15-W4,10 in E. coli achieved increased recombinant peptide yield through multiple tandem copies per fusion protein — a scalable manufacturing approach for commercial antimicrobial peptide production.
Why it matters
Relevant for antimicrobial-peptides, peptide-design.
How the study worked
in-vitro study.
What this study cannot tell us
See abstract.
How to read the evidence
preliminary evidence.
When this study was published
Published in 2007.
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
Multimerization and fusion expression of bovine lactoferricin derivative LfcinB15-W4,10 in Escherichia coli.
Applied microbiology and biotechnology, 75(1), 117-24
Citation
Tian, Zi-Gang; Teng, Da; Yang, Ya-Lin; Luo, Jin; Feng, Xing-Jun; Fan, Ying; Zhang, Fan; Wang, Jian-Hua. (2007). Multimerization and fusion expression of bovine lactoferricin derivative LfcinB15-W4,10 in Escherichia coli.. Applied microbiology and biotechnology, 75(1), 117-24.