The antifungal activity of lactoferrampin was mapped to a specific cluster of positively charged residues, with mutations reducing charge eliminating candidacidal activity — electrostatic interaction drives yeast killing.
Key findingLactoferrampin's candidacidal activity was localized to a cluster of positively charged residues that interact electrostatically with negatively charg
What the researchers found
Lactoferrampin's candidacidal activity was localized to a cluster of positively charged residues that interact electrostatically with negatively charged yeast membranes, with charge-reducing mutations eliminating activity — defining the minimal antifungal pharmacophore.
Why it matters
Relevant for antimicrobial-peptides, infection, peptide-design.
How the study worked
in-vitro study on antimicrobial-peptides, infection.
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/biomarker research.
Questions still open
- Further research needed.
- Clinical translation to evaluate.
Common questions
What was studied?
What was found?
Read the original research
Lactoferrampin, an antimicrobial peptide of bovine lactoferrin, exerts its candidacidal activity by a cluster of positively charged residues at the C-terminus in combination with a helix-facilitating N-terminal part.
Biological chemistry, 386(2), 137-42
Citation
van der Kraan, Marieke I A; Nazmi, Kamran; Teeken, Afke; Groenink, Jasper; van 't Hof, Wim; Veerman, Enno C I; Bolscher, Jan G M; Nieuw Amerongen, Arie V. (2005). Lactoferrampin, an antimicrobial peptide of bovine lactoferrin, exerts its candidacidal activity by a cluster of positively charged residues at the C-terminus in combination with a helix-facilitating N-terminal part.. Biological chemistry, 386(2), 137-42.