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LL-37

Cathelicidin, hCAP-18, FALL-39, CAP-18

Quick Stats
Studies 2230
Trials 95
Score 2
2012 pubmed 25 citations

Defense peptides secreted by helminth pathogens: antimicrobial and/or immunomodulator molecules?

Cotton. Sophie S; Donnelly. Sheila S; Robinson. Mark W MW; Dalton. John P JP; Thivierge. Karine K

Key Findings

  • Helminths produce peptides structurally similar to human LL‑37
  • These peptides have both antimicrobial and immunomodulatory effects
  • The similarity may allow the worms to mimic host defenses and dampen inflammation

Practical Outcomes

  • At this stage there’s no direct protocol to try, but the findings hint that peptide‑based anti‑inflammatory tools could be developed in the future. For now, biohackers should treat this as interesting background science rather than a ready‑to‑use supplement.

Summary

Scientists found that some worm parasites make tiny proteins that look a lot like the human immune peptide LL‑37. These worm‑derived peptides can kill microbes and also tweak the immune system, possibly explaining why worm infections sometimes reduce inflammation. The study is basic research and doesn’t give any dosage or supplement advice for everyday use.

Abstract

Host defense peptides (HDPs) are an evolutionarily conserved component of the innate immune response found in all living species. They possess antimicrobial activities against a broad range of organisms including bacteria, fungi, eukaryotic parasites, and viruses. HDPs also have the ability to enhance immune responses by acting as immunomodulators. We discovered a new family of HDPs derived from pathogenic helminth (worms) that cause enormous disease in animals and humans worldwide. The discovery of these peptides was based on their similar biochemical and functional characteristics to the human defense peptide LL-37. We propose that these new peptides modulate the immune response via molecular mimicry of mammalian HDPs thus providing a mechanism behind the anti-inflammatory properties of helminth infections.

Study Information

Provider

pubmed

Year

2012

Date

2012-08-28T00:00:00.000Z

DOI

10.3389/fimmu.2012.00269

Citations

25

References

99