Anti-human immunodeficiency virus type 1 activities of antimicrobial peptides derived from human and bovine cathelicidins.
Wang. Guangshun G; Watson. Karen M KM; Buckheit. Robert W RW
Key Findings
- FK‑13 is the smallest LL‑37‑derived peptide that still blocks HIV.
- GI‑20 has the highest therapeutic index (effectiveness vs. toxicity), twice that of the full‑length LL‑37.
- BMAP‑18, from bovine cathelicidin, matches GI‑20’s therapeutic index.
- Peptide sequence order, helical structure, and aromatic residues are crucial for HIV inhibition.
Practical Outcomes
- For DIY biohackers, these results suggest that very short, well‑designed peptide fragments might be more effective and safer than using the whole LL‑37 protein for antiviral purposes. However, the peptides are not commercially available, and safety in humans is unproven, so any self‑experimentation would be highly experimental and should be approached with caution.
Summary
Scientists tested short pieces of the natural protein LL‑37 and a similar bovine protein to see if they can block HIV. They found that a tiny fragment called FK‑13 can stop the virus, while another fragment, GI‑20, works best with the fewest side effects. A bovine‑derived peptide, BMAP‑18, performed about as well as GI‑20. The shape and certain amino acids of these peptides are key to their antiviral action.
Abstract
From among 15 human cathelicidin LL-37-derived peptides, FK-13 was identified as the smallest peptide active against human immunodeficiency virus (HIV) and GI-20 had the highest therapeutic index, which was twice that of LL-37. BMAP-18, which is derived from bovine cathelicidin BMAP-27, possessed a therapeutic index similar to that of GI-20. Peptide sequence order, helical structures, and aromatic residues are important in HIV inhibition.
Study Information
pubmed
2008
2008-06-30T00:00:00.000Z
10.1128/aac.00452-08