Acylated tryptophan-methylated lactoferricin peptides showed enhanced lipid membrane insertion by solid-state NMR, explaining how chemical modifications improve antimicrobial potency at the molecular interaction level.
Key findingSolid-state NMR revealed acylated, tryptophan-methylated lactoferricin peptides inserted deeper into lipid bilayers with stronger membrane disruption,
What the researchers found
Solid-state NMR revealed acylated, tryptophan-methylated lactoferricin peptides inserted deeper into lipid bilayers with stronger membrane disruption, providing molecular-level explanation for how chemical modifications enhance antimicrobial potency.
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 2008.
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
Lipid interactions of acylated tryptophan-methylated lactoferricin peptides by solid-state NMR.
Journal of peptide science : an official publication of the European Peptide Society, 14(10), 1103-10
Citation
Greathouse, Denise; Vostrikov, Vitaly; McClellan, Nicole; Chipollini, Juan; Lay, Jack; Liyanage, Rohana; Ladd, Taylor. (2008). Lipid interactions of acylated tryptophan-methylated lactoferricin peptides by solid-state NMR.. Journal of peptide science : an official publication of the European Peptide Society, 14(10), 1103-10. https://doi.org/10.1002/psc.1047