Human lactoferricin is partially folded in water but stabilizes into its active antimicrobial conformation at membrane-like surfaces — the membrane environment activates its structure for bacterial killing.
Key findingNMR studies showed human lactoferricin adopts a partially structured conformation in water that stabilizes into an amphipathic beta-hairpin at membran
What the researchers found
NMR studies showed human lactoferricin adopts a partially structured conformation in water that stabilizes into an amphipathic beta-hairpin at membrane-mimetic surfaces, revealing that the bacterial membrane itself activates the peptide's antimicrobial structure.
Why it matters
Relevant for antimicrobial-peptides, peptide-design, infection.
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 2005.
The bigger picture
Advances peptide research with clinical implications.
Questions still open
- Further research needed.
- Clinical translation to evaluate.
Common questions
What was studied?
What was found?
Read the original research
Human lactoferricin is partially folded in aqueous solution and is better stabilized in a membrane mimetic solvent.
Antimicrobial agents and chemotherapy, 49(8), 3387-95
Citation
Hunter, Howard N; Demcoe, A Ross; Jenssen, Håvard; Gutteberg, Tore J; Vogel, Hans J. (2005). Human lactoferricin is partially folded in aqueous solution and is better stabilized in a membrane mimetic solvent.. Antimicrobial agents and chemotherapy, 49(8), 3387-95.