Cathelicidin Fragments and D-Enantiomers: Designing Better Antimicrobial Peptides

What the researchers found

Study of cathelicidin PMAP-36 and BMAP-27 fragments plus D-enantiomers reveals design strategies for more stable, potent antimicrobial peptides.

Why it matters

These findings have significant implications for peptide-based therapeutic development and clinical practice.

The numbers in context

Two peptide fragments tested: PMAP(12-24) and BMAP(1-18), plus their all-D-amino acid enantiomers. Tested for antimicrobial activity and protease resistance.

How the study worked

Study design and methodology detailed in the full publication.

Who was studied

In vitro testing against bacterial panels

What this study cannot tell us

Study-specific limitations discussed in the full publication. Results should be interpreted within the context of study design.

How to read the evidence

Evidence assessment based on study design detailed in publication.

When this study was published

Published in 2025. Current peptide therapeutic research.

The bigger picture

This study contributes to the expanding understanding of how peptide-based therapeutics can be applied across medical specialties.

Questions still open

• What are the long-term implications?
• How do these results compare to existing evidence?
• What further research is needed?

Common questions

Read the original research

Fragments of cathelicidins PMAP-36 and BMAP-27 and their D-enantiomers: Effects of all D substitutions on structure, protease resistance and antimicrobial properties.

Bioorganic chemistry, 163, 108715

Citation

Albini, Francesca; Biondi, Barbara; Di Stasi, Adriana; Schivo, Andrea; Mardirossian, Mario; Scocchi, Marco; Peggion, Cristina. (2025). Fragments of cathelicidins PMAP-36 and BMAP-27 and their D-enantiomers: Effects of all D substitutions on structure, protease resistance and antimicrobial properties.. Bioorganic chemistry, 163, 108715. https://doi.org/10.1016/j.bioorg.2025.108715