Antimicrobial activity of Tachyplesin 1 against <i>Burkholderia pseudomallei</i>: an in vitro and in silico approach.
Lee. Lyn-Fay LF; Mariappan. Vanitha V; Vellasamy. Kumutha Malar KM; Lee. Vannajan Sanghiran VS; Vadivelu. Jamuna J
Key Findings
- LL‑37 and PG‑1 showed 100% activity against B. pseudomallei in planktonic form; TP1 showed 83% activity.
- TP1 killed the bacteria within 2 hours and disrupted their membranes, but was toxic to mammalian cell lines.
- TP1 could reduce bacterial biofilm growth at concentrations above 221 µM, but its cytotoxicity limits practical use.
Practical Outcomes
- For biohackers, LL‑37 remains a promising antimicrobial peptide, but the study provides no dosing guidance or safety data for human use. TP1’s strong antibacterial effect is offset by its toxicity, making it unsuitable for self‑experimentation without further modification. The findings mainly highlight the need for safety testing before considering any peptide as a DIY antimicrobial supplement.
Summary
The study tested several natural antimicrobial peptides against the tough bacteria Burkholderia pseudomallei. While LL‑37 and PG‑1 killed all tested strains, the researchers focused on another peptide, Tachyplesin 1 (TP1), which also killed the bacteria quickly but also harmed human cells in lab tests.
Abstract
<i>Burkholderia pseudomallei</i>, the causative agent of melioidosis, is intrinsically resistant to many conventional antibiotics. Therefore, alternative antimicrobial agents such as antimicrobial peptides (AMPs) are extensively studied to combat this issue. Our study aims to identify and understand the mode of action of the potential AMP(s) that are effective against <i>B. pseudomallei</i> in both planktonic and biofilm state as well as to predict the possible binding targets on using in vitro and in silico approaches. In the in vitro study, 11 AMPs were tested against 100 <i>B. pseudomallei</i> isolates for planktonic cell susceptibility, where LL-37, and PG1, demonstrated 100.0% susceptibility and TP1 demonstrated 83% susceptibility. Since the <i>B. pseudomallei</i> activity was reported on LL-37 and PG1, TP1 was selected for further investigation. TP1 inhibited <i>B. pseudomallei</i> cells at 61.69 μM, and membrane blebbing was observed using scanning electron microscopy. Moreover, TP1 inhibited <i>B. pseudomallei</i> cell growth, reaching bactericidal endpoint within 2 h post exposure as compared to ceftazidime (CAZ) (8 h). Furthermore, TP1 was shown to suppress the growth of <i>B. pseudomallei</i> cells in biofilm state at concentrations above 221 μM. However, TP1 was cytotoxic to the mammalian cell lines tested. In the in silico study, molecular docking revealed that TP1 demonstrated a strong interaction to the common peptide or inhibitor binding targets for lipopolysaccharide of <i>Escherichia coli</i>, as well as autolysin, pneumolysin, and pneumococcal surface protein A (PspA) of <i>Streptococcus pneumoniae</i>. Homology modelled <i>B. pseudomallei</i> PspA protein (YDP) also showed a favourable binding with a strong electrostatic contribution and nine hydrogen bonds. In conclusion, TP1 demonstrated a good potential as an anti-<i>B. pseudomallei</i> agent.
Study Information
pubmed
2016
2016-10-25T00:00:00.000Z
10.7717/peerj.2468
8
86