Study type: Human research · Status: Verified against declared source
Studies on citrullinated LL-37: detection in human airways, antibacterial effects and biophysical properties.
Scientific reports · 2020
Study scale: Not reported
Abstract only: Open source record
Product or molecular entity relationships
- LL-37: Exact entity relationship. Legacy citation custody associates this source with the catalog record; no product-relevance conclusion is implied.
Plain-language verified summary
Question
Arginine residues of the antimicrobial peptide LL-37 can be citrullinated by peptidyl arginine deiminases, which reduce the positive charge of the peptide.
Methods
Given the broad specificity of PAD enzymes and its co-expression during inflammation in the lungs, it is reasonable to suggest that LL-37 can serve as a substrate for PAD-activity in the lungs.
Scale or participants
Not reported in the reviewed source.
Key findings
Arginine residues of the antimicrobial peptide LL-37 can be citrullinated by peptidyl arginine deiminases, which reduce the positive charge of the peptide.
Limitations and uncertainty
Arginine residues of the antimicrobial peptide LL-37 can be citrullinated by peptidyl arginine deiminases, which reduce the positive charge of the peptide.
Verified against declared source. Verification is limited to the declared source and review scope. It does not mean independent replication or establish efficacy, safety, or suitability.