LL-37 fragments have antimicrobial activity against Staphylococcus epidermidis biofilms and wound healing potential in HaCaT cell line.
Saporito. Paola P; Vang Mouritzen. Michelle M; Løbner-Olesen. Anders A; Jenssen. Håvard H
Key Findings
- KR‑12 and VQ‑12V26 12‑mer fragments inhibit and eradicate S. epidermidis biofilms more effectively than full‑length LL‑37
- These fragments show reduced cytotoxicity toward human keratinocytes and erythrocytes
- Both KR‑12 and VQ‑12V26 enhance wound‑healing activity in HaCaT skin cell cultures, with VQ‑12 gaining function from a single amino‑acid substitution
Practical Outcomes
- The key takeaway is that short LL‑37‑derived peptides may serve as safer, potent topical agents for fighting biofilm‑related skin infections and boosting wound repair. However, they are still laboratory findings; further formulation, dosing, and safety studies are needed before they can be used by biohackers or consumers.
Summary
Researchers found that tiny pieces of the natural antimicrobial peptide LL‑37, especially KR‑12 and a modified version called VQ‑12V26, can better stop and break down Staphylococcus epidermidis biofilms, are gentler on skin cells and red blood cells, and even help skin cells heal faster in lab dishes. These findings hint that short peptide fragments could become safer, more effective topical treatments for wound care and infection prevention, though they’re still early‑stage and not yet ready for DIY use.
Abstract
Staphylococcus epidermidis is a common nosocomial pathogen able to form biofilms in indwelling devices, resulting in chronic infections, which are refractory to antibiotics treatment. Staphylococcal biofilms are also associated with the delayed reepithelization and healing of chronic wounds. The human cathelicidin peptide LL-37 has been proven active against S. epidermidis biofilms in vitro and to promote wound healing. As previous studies have demonstrated that fragments of LL-37 could possess an equal antibacterial activity as the parent peptide, we tested whether shorter (12-mer) synthetic fragments of LL-37 maintained the antibiofilm and/or immune modulating activity, aiming at the identification of essential regions within the LL-37 parent sequence. Three fragments of LL-37 displayed improved activity against S. epidermidis in terms of biofilm inhibition and eradication, a reduced cytotoxicity to human keratinocytes and erythrocytes. In addition, KR-12 and VQ-12<sup>V26</sup> enhanced wound healing potential, relative to LL37. FK-12 and KR-12 are truncated version of the cathelicidin, previously reported as valid antimicrobials, whereas VQ-12<sup>V26</sup> is a single substituted LL-37 fragment. Remarkably, the single substitution aspartic acid to valine in position 26 caused gain of antimicrobial function in the inactive VQ-12 fragment. The combination of antibiofilm, wound healing potential, and low cytotoxicity makes KR-12 and VQ-12<sup>V26</sup> promising therapeutic agents and lead compounds for further improvement and understanding of antibiofilm and wound healing properties.
Study Information
pubmed
2018
2018-05-08T00:00:00.000Z
10.1002/psc.3080
47
40