Human Lactoferricin's Structure: Partially Folded in Water, Fully Active at Membranes
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.
Quick Facts
What This Study 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.
Key Numbers
How They Did This
in-vitro study on antimicrobial-peptides, peptide-design.
Why This Research Matters
Relevant for antimicrobial-peptides, peptide-design, infection.
The Bigger Picture
Advances peptide research with clinical implications.
What This Study Doesn't Tell Us
See abstract.
Questions This Raises
- ?Further research needed.
- ?Clinical translation to evaluate.
Trust & Context
- Key Stat:
- Key finding NMR studies showed human lactoferricin adopts a partially structured conformation in water that stabilizes into an amphipathic beta-hairpin at membran
- Evidence Grade:
- preliminary evidence.
- Study Age:
- Published in 2005.
- Original Title:
- Human lactoferricin is partially folded in aqueous solution and is better stabilized in a membrane mimetic solvent.
- Published In:
- Antimicrobial agents and chemotherapy, 49(8), 3387-95 (2005)
- Authors:
- Hunter, Howard N, Demcoe, A Ross, Jenssen, Håvard(3), Gutteberg, Tore J, Vogel, Hans J
- Database ID:
- RPEP-01048
Evidence Hierarchy
Frequently Asked Questions
What was studied?
Human Lactoferricin's Structure: Partially Folded in Water, Fully Active at Membranes
What was found?
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.
Read More on RethinkPeptides
Cite This Study
https://rethinkpeptides.com/research/RPEP-01048APA
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.
MLA
Hunter, Howard N, et al. "Human lactoferricin is partially folded in aqueous solution and is better stabilized in a membrane mimetic solvent.." Antimicrobial agents and chemotherapy, 2005.
RethinkPeptides
RethinkPeptides Research Database. "Human lactoferricin is partially folded in aqueous solution ..." RPEP-01048. Retrieved from https://rethinkpeptides.com/research/hunter-2005-human-lactoferricin-is-partially
Access the Original Study
Study data sourced from PubMed, a service of the U.S. National Library of Medicine, National Institutes of Health.
This study breakdown was produced by the RethinkPeptides research team. We analyze and report published research findings without making health recommendations. All interpretations are based solely on the published abstract and study data.