Systematic C- and N-terminal truncation of lactoferrampin (LFampin 265-284) revealed the minimal active sequence needed for antimicrobial activity versus biophysical membrane interaction — not all structure-activity matches.
Key findingSystematic C- and N-terminal truncation of lactoferrampin (LFampin 265-284) revealed the minimal active sequence needed for antimicrobial activity ver
What the researchers found
Systematic C- and N-terminal truncation of lactoferrampin (LFampin 265-284) revealed the minimal active sequence needed for antimicrobial activity versus biophysical membrane interaction — not all structure-activity matches.
Why it matters
Relevant for peptide research.
How the study worked
research study.
What this study cannot tell us
See abstract.
How to read the evidence
emerging evidence.
When this study was published
Published in 2011.
The bigger picture
Advances peptide research.
Questions still open
- Further research needed.
Common questions
What was studied?
What was found?
Read the original research
C- and N-truncated antimicrobial peptides from LFampin 265 - 284: Biophysical versus microbiology results.
Journal of pharmacy & bioallied sciences, 3(1), 60-9
Citation
Adão, Regina; Nazmi, Kamran; Bolscher, Jan G M; Bastos, Margarida. (2011). C- and N-truncated antimicrobial peptides from LFampin 265 - 284: Biophysical versus microbiology results.. Journal of pharmacy & bioallied sciences, 3(1), 60-9. https://doi.org/10.4103/0975-7406.76467