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LL-37

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

Quick Stats
Studies 2230
Trials 95
Score 3
2016 pubmed

[Prokaryotic expression and purification of antimicrobial peptide LL-37 and the inhibiting effect against Candida albicans].

Huo. Y Y; Wang. F F; Sun. B B; Yin. L R LR; Zhang. P P PP; Zhang. Y J YJ; Zhang. B M BM

Key Findings

  • Recombinant LL‑37 protein (ā‰ˆ434 µg/mL, 96% pure) displayed clear antifungal activity against Candida albicans in a standard disk diffusion test.
  • When added to a co‑culture of human vaginal epithelial cells and Candida, LL‑37 significantly reduced yeast growth over 12‑48 hours compared to untreated controls.
  • LL‑37 treatment increased IFN‑γ levels and decreased IL‑10 levels in the epithelial cells, raising the IFN‑γ/IL‑10 ratio, indicating a shift toward a more antifungal immune environment.

Practical Outcomes

  • The study suggests that boosting LL‑37 locally could help control vaginal yeast infections by both directly inhibiting the fungus and enhancing the tissue’s immune response. For DIY health enthusiasts, this points to the potential of topical LL‑37 formulations, but note that the peptide was produced in a lab setting and isn’t currently available as a consumer product. More work is needed to translate these findings into safe, effective at‑home protocols.

Summary

Researchers made a lab‑produced version of the natural peptide LL‑37 and showed it can slow down Candida yeast growth in a dish that mimics the vagina. The peptide also boosted a ā€œgoodā€ immune signal (IFN‑γ) and lowered an anti‑inflammatory signal (IL‑10), which together may help the tissue fight infection.

Abstract

To study the inhibitory effect of antimicrobial peptide LL-37 on Candida albicans through its ability to promote the secretion of immune factors by vaginal epithelial cells. (1) LL-37 prokaryotic expression vector pET-Duet/LL-37 was constructed and its expression was induced in Escherichia coli M15. The expressed LL-37 fusion protein was purified and identified by western blot. Antifungal activity of the purified protein was initially identified by Kirby-Bauer (K-B) method. (2) Purified LL-37 protein was added to human vaginal epithelial cells co-cultured with Candida, and inhibitory effect on Candida growth was determined by the glucose consumption method. Interferon γ (IFN-γ), interleukin 10 (IL-10) concentration and IFN-γ/IL-10 ratio were measured by ELISA at different time points. (1) LL-37 fusion protein was purified to 96% purity at a concentration of 433.92 μg/ml, and was shown to possess anti-fungal activity confirmed by the K-B method. (2) A Candida-vaginal epithelial cells co-culture system was successfully constructed. LL-37 recombinant protein inhibited the growth of Candida with absorbance values significantly higher in the treatment group compared to the control group at all measured time points (12-hour: 3.008±0.003 versus 2.967±0.003, 24-hour: 2.941±0.003 versus 2.601±0.003, 48-hour: 2.893 ± 0.004 versus 2.409 ± 0.003; all P<0.01). Furthermore, the rate of decrease was also much slower compared to the control group. In both control and experimental groups, IFN-γ and IL-10 secretion levels were observed to rise at first peaking at 24 hours and subsequently decrease. For each time period, IFN-γ concentration in the experimental group was significantly higher at 24 hours compared to the control group [(104.00 ± 1.07) versus (85.17 ± 0.28) pg/ml,P<0.01]. In contrast, IL-10 concentrations were significantly lower than the control group at all time points (P<0.01). IFN-γ/IL-10 ratio was also observed to be significantly higher than the control group at all measured time points (P<0.01). (1) Recombinant protein LL-37 could significantly inhibit the growth of Candida. (2) By influencing the secretion of immune factors such as IFN-γ, IL-10, etc, recombinant protein LL-37 is able to adjust vaginal epithelial cells local immunity, and enhance resistance to Candida infection.

Study Information

Provider

pubmed

Year

2016

DOI

10.3760/cma.j.issn.0529-567x.2016.02.008