Truncating Lactoferrampin Peptide: Which Parts Are Essential for Antimicrobial Activity?

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.

Adão, Regina et al.·Journal of pharmacy & bioallied sciences·2011·
RPEP-017282011RETHINKTHC RESEARCH DATABASErethinkthc.com/research

Quick Facts

Study Type
Not classified
Evidence
Not graded
Sample
Not reported

What This Study 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.

Key Numbers

How They Did This

research study.

Why This Research Matters

Relevant for peptide research.

The Bigger Picture

Advances peptide research.

What This Study Doesn't Tell Us

See abstract.

Questions This Raises

  • ?Further research needed.

Trust & Context

Key Stat:
Key finding Systematic C- and N-terminal truncation of lactoferrampin (LFampin 265-284) revealed the minimal active sequence needed for antimicrobial activity ver
Evidence Grade:
emerging evidence.
Study Age:
Published in 2011.
Original Title:
C- and N-truncated antimicrobial peptides from LFampin 265 - 284: Biophysical versus microbiology results.
Published In:
Journal of pharmacy & bioallied sciences, 3(1), 60-9 (2011)
Database ID:
RPEP-01728

Evidence Hierarchy

Meta-Analysis / Systematic Review
Randomized Controlled Trial
Cohort / Case-Control
Cross-Sectional / ObservationalSnapshot without intervening
This study
Case Report / Animal Study
What do these levels mean? →

Frequently Asked Questions

What was studied?

Truncating Lactoferrampin Peptide: Which Parts Are Essential for Antimicrobial Activity?

What was 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.

Read More on RethinkPeptides

Related articles coming soon.

Cite This Study

RPEP-01728·https://rethinkpeptides.com/research/RPEP-01728

APA

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

MLA

Adão, Regina, et al. "C- and N-truncated antimicrobial peptides from LFampin 265 - 284: Biophysical versus microbiology results.." Journal of pharmacy & bioallied sciences, 2011. https://doi.org/10.4103/0975-7406.76467

RethinkPeptides

RethinkPeptides Research Database. "C- and N-truncated antimicrobial peptides from LFampin 265 -..." RPEP-01728. Retrieved from https://rethinkpeptides.com/research/adao-2011-c-and-ntruncated-antimicrobial

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.