Evaluation of the inactivation of infectious Herpes simplex virus by host-defense peptides.
Yasin. B B; Pang. M M; Turner. J S JS; Cho. Y Y; Dinh. N N NN; Waring. A J AJ; Lehrer. R I RI; Wagar. E A EA
Key Findings
- LL‑37 showed little to no ability to inactivate HSV‑1 or HSV‑2 in vitro
- Beta‑sheet peptides like defensins, tachyplesin, and protegrins could inactivate one or both HSV types, sometimes selectively
- Indolicidin and brevinin‑1 were the only peptides that blocked both HSV‑1 and HSV‑2, and brevinin‑1 kept activity after modifications that removed its toxicity
Practical Outcomes
- For DIY health enthusiasts, LL‑37 isn’t a viable anti‑herpes agent, so don’t invest in it for that purpose. If you’re exploring peptide antivirals, beta‑sheet peptides show more promise, but many are cytotoxic and need careful handling. Brevinin‑1 could be a lead compound, though it still requires further safety and efficacy testing before practical use.
Summary
The study found that LL‑37, a common human antimicrobial peptide, barely stopped herpes simplex virus (HSV‑1 or HSV‑2) from infecting cells, so it isn’t useful as an anti‑herpes supplement. Some other natural peptides did work, but many are toxic or need more research.
Abstract
A 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide microplate assay was adapted to screen for the ability of 20 host-defense peptides to inactivate herpes simplex virus type 1 and type 2. The procedure required minimal amounts of material, was reproducible, and was confirmed with standard antiviral testing techniques. In screening tests, with the exception of melittin, a highly cytotoxic and hemolytic peptide found in bee venom, the alpha-helical peptides in our test panel (magainins, cecropins, clavanins, and LL-37) caused little viral inactivation. Several beta-sheet peptides (defensins, tachyplesin, and protegrins) inactivated one or both viruses, sometimes with remarkable selectivity. Two peptides were identified as having antiviral activity against both viruses, indolicidin (a tryptophan-rich peptide from bovine neutrophils) and brevinin-1 (a peptide found in frog skin). The antiviral activity of these two peptides was confirmed with standard antiviral assays. Interestingly, the antiviral activity of brevinin-1 was maintained after reduction and carboxamidomethylation, procedures that abolished its otherwise prominent hemolytic and cytotoxic effects.
Study Information
pubmed
2000
10.1007/s100960050457
213
49