N-acylation (adding fatty acid chains) of a human lactoferricin-derived peptide improved its selectivity for bacterial membranes over human cell membranes — a chemical modification strategy for safer antimicrobial peptides.
Key findingN-acylation of a human lactoferricin-derived peptide improved membrane selectivity: maintaining or enhancing antibacterial activity while reducing tox
What the researchers found
N-acylation of a human lactoferricin-derived peptide improved membrane selectivity: maintaining or enhancing antibacterial activity while reducing toxicity to human cells — demonstrating lipid modification as a strategy for improving antimicrobial peptide therapeutic windows.
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
Influence of N-acylation of a peptide derived from human lactoferricin on membrane selectivity.
Biochimica et biophysica acta, 1758(9), 1426-35
Citation
Zweytick, Dagmar; Pabst, Georg; Abuja, Peter M; Jilek, Alexander; Blondelle, Sylvie E; Andrä, Jörg; Jerala, Roman; Monreal, Daniel; Martinez de Tejada, Guillermo; Lohner, Karl. (2006). Influence of N-acylation of a peptide derived from human lactoferricin on membrane selectivity.. Biochimica et biophysica acta, 1758(9), 1426-35.