An enhanced bovine lactoferricin variant (LfcinB-W10) was expressed and purified from E. coli with retained antimicrobial activity — manufacturing the optimized peptide for practical antimicrobial use.
Key findingAn enhanced bovine lactoferricin variant (LfcinB-W10) was expressed and purified from E. coli with retained antimicrobial activity — manufacturing the
What the researchers found
An enhanced bovine lactoferricin variant (LfcinB-W10) was expressed and purified from E. coli with retained antimicrobial activity — manufacturing the optimized peptide for practical antimicrobial use.
Why it matters
Relevant for peptide research.
How the study worked
research study.
What this study cannot tell us
See abstract.
How to read the evidence
emerging evidence.
When this study was published
Published in 2010.
The bigger picture
Advances peptide research.
Questions still open
- Further research needed.
Common questions
What was studied?
What was found?
Read the original research
Expression and purification of an antimicrobial peptide, bovine lactoferricin derivative LfcinB-W10 in Escherichia coli.
Current microbiology, 60(3), 179-84
Citation
Feng, Xingjun; Liu, Chunlong; Guo, Jiayin; Bi, Chongpeng; Cheng, Baojing; Li, Zhongyu; Shan, Anshan; Li, Zhongqiu. (2010). Expression and purification of an antimicrobial peptide, bovine lactoferricin derivative LfcinB-W10 in Escherichia coli.. Current microbiology, 60(3), 179-84. https://doi.org/10.1007/s00284-009-9522-8