Development of novel LL-37 derived antimicrobial peptides with LPS and LTA neutralizing and antimicrobial activities for therapeutic application.
Nell. Marja J MJ; Tjabringa. G Sandra GS; Wafelman. Amon R AR; Verrijk. Ruud R; Hiemstra. Pieter S PS; Drijfhout. Jan W JW; Grote. Jan J JJ
Key Findings
- P60.4, a 24‑amino‑acid LL‑37 derivative, matches LL‑37 in neutralizing LPS and LTA
- P60.4 triggers less pro‑inflammatory activity than LL‑37
- Acetylated and amidated P60.4 shows no toxicity and keeps equal or better antimicrobial power
Practical Outcomes
- This work suggests that short, stabilized LL‑37‑like peptides could become safer, more effective treatments for respiratory infections, but they are not yet available for personal use. Biohackers should watch for future clinical trials or commercial products based on these designs, rather than trying them now.
Summary
Researchers made new short versions of the human peptide LL-37, especially one called P60.4, that can neutralize bacterial toxins (LPS and LTA) as well as the original peptide but cause less inflammation, and the chemically tweaked version appears safe and still kills microbes.
Abstract
New peptides for lipopolysaccharide (LPS) and lipoteichoic acid (LTA) neutralization in upper respiratory tract infections were developed and evaluated in terms of efficacy and safety for application in humans. Based on the sequence of the human antimicrobial peptide LL-37 we developed and investigated length variants, substitution analogues and modifications to stabilize the peptides to prevent enzymatic degradation and to improve efficacy. The most promising peptide appears P60.4, a 24 amino acid peptide with similar efficacy as LL-37 in terms of LPS and LTA neutralization and lower pro-inflammatory activity. In addition, the acetylated and amidated version of this peptide shows no toxicity and displays higher or equal antimicrobial activity compared to LL-37.
Study Information
pubmed
2005
2005-11-07T00:00:00.000Z
10.1016/j.peptides.2005.09.016
175
49