Degradation of naturally occurring and engineered antimicrobial peptides by proteases.
Moncla. Bernard J BJ; Pryke. Kara K; Rohan. Lisa Cencia LC; Graebing. Phillip W PW
Key Findings
- LL-37 is the most sensitive of the tested peptides to protease digestion.
- Two anaerobic vaginal bacteria (Prevotella bivia and Porphyromonas asaccharolytica) can also degrade LL-37.
- Most antimicrobial peptides, including LL-37, may have short lifespans in protease‑rich environments.
Practical Outcomes
- For DIY health enthusiasts, LL-37 probably isn’t effective when taken orally or applied where enzymes are abundant. To use it, you’d need a delivery system that protects the peptide (e.g., encapsulation, nasal spray, or topical formulation with enzyme inhibitors). This info helps you avoid wasted doses and focus on more stable alternatives.
Summary
The study shows that the antimicrobial peptide LL-37 breaks down quickly when exposed to common proteases and certain vaginal bacteria, meaning it likely won’t stay intact for long in places in the body that have lots of digestive enzymes.
Abstract
We hypothesized that current antimicrobial peptides should be susceptible to proteolytic digestion. The antimicrobial peptides: Griffithinsin, RC-101, LL-37, LSA-5, PSC-RANTES and DJ007 were degraded by commercially available proteases. Two different species of anaerobic vaginal flora, Prevotella bivia and Porphyromonas asaccharolytica also degraded the materials. Griffithsin was resistant to digestion by 8 of the 9 proteases and the bacteria while LL-37 was the most sensitive to protease digestion. These data suggests most of the molecules may not survive for very long in the proteolytic rich environments in which they are intended to function.
Study Information
pubmed
2011
10.4236/abb.2011.26059