NMR structural comparison of 15-residue lactoferricin variants in membrane environments revealed specific structural features correlated with antimicrobial potency — helix amphipathicity and membrane insertion depth determine killing ability.
Key findingNMR comparison of 15-residue lactoferricin-derived peptides in membrane-mimetic environments showed helix amphipathicity and depth of membrane inserti
What the researchers found
NMR comparison of 15-residue lactoferricin-derived peptides in membrane-mimetic environments showed helix amphipathicity and depth of membrane insertion correlated with antimicrobial activity — structural determinants of killing potency identified.
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
Comparison of NMR structures and model-membrane interactions of 15-residue antimicrobial peptides derived from bovine lactoferricin.
Biochemistry and cell biology = Biochimie et biologie cellulaire, 84(3), 312-26
Citation
Jing, Weiguo; Svendsen, John S; Vogel, Hans J. (2006). Comparison of NMR structures and model-membrane interactions of 15-residue antimicrobial peptides derived from bovine lactoferricin.. Biochemistry and cell biology = Biochimie et biologie cellulaire, 84(3), 312-26.