Schillaci D et al. (2014), Paracentrin 1, a synthetic antimicrobial peptid...

ECB-ART-43694

AMB Express 2014 Oct 31;4:78. doi: 10.1186/s13568-014-0078-z.

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Paracentrin 1, a synthetic antimicrobial peptide from the sea-urchin Paracentrotus lividus, interferes with staphylococcal and Pseudomonas aeruginosa biofilm formation.

Schillaci D , Cusimano MG , Spinello A , Barone G , Russo D , Vitale M , Parrinello D , Arizza V .

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The rise of antibiotic-resistance as well as the reduction of investments by pharmaceutical companies in the development of new antibiotics have stimulated the investigation for alternative strategies to conventional antibiotics. Many antimicrobial peptides show a high specificity for prokaryotes and a low toxicity for eukaryotic cells and, due to their mode of action the development of resistance is considered unlikely. We recently characterized an antimicrobial peptide that was called Paracentrin 1 from the 5-kDa peptide fraction from the coelomocyte cytosol of the Paracentrotus lividus. In this study, the chemically synthesized Paracentrin 1, was tested for its antimicrobial and antibiofilm properties against reference strains of Gram positive and Gram negative. The Paracentrin 1 was active against planktonic form of staphylococcal strains (reference and isolates) and Pseudomonas aeruginosa ATCC 15442 at concentrations ranging from 12.5 to 6.2 mg/ml. The Paracentrin 1 was able to inhibit biofilm formation of staphylococcal and Pseudomonas aeruginosa strains at concentrations ranging from 3.1 to 0.75 mg/ml. We consider the tested peptide as a good starting molecule for novel synthetic derivatives with improved pharmaceutical potential.

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Genes referenced: LOC100887844

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References [+] :

Andreu, Animal antimicrobial peptides: an overview. 1998, Pubmed

	Figure 1. Example of MD simulation box, showing the SP1 molecule, the solution counterions, Na + (in blue) and Cl âˆ’ (in cyan), and the explicit water molecules (in red).
	Figure 2. Plot of the RMSD obtained for SP1 up to 400Â ns of MD simulation.
	Figure 3. Ramachandran plot showing the values of psi and phi angles assumed by residues 2â€“10 of SP1 between 150 and 250Â ns of the MD simulation.
	Figure 4. Molecular representation of SP1 at about 200Â ns of MD showing the non amphipathic structure of the peptide. The potential surface is superimposed. Color code: acidic residues in red, basic residues in blue, and hydrophobic residues in yellow.
	Figure 5. Interference with biofilm formation of SP1 against reference staphylococcal andP. aeruginosastrains. The percentage of inhibition were evaluated comparing the samples with not-treated 24Â h old biofilms and staining with safranin. Bacterial strains () S. aureus 25923, () S. aureus 29213, () S. aureus 6538, () S. epidermidis RP62A, () P. aeruginosa 15442. Data for each strain are the mean of three distinct experimentsâ€‰Â±â€‰S.D.
	Figure 6. SEM micrography showing the effect of sub-MIC concentration of SP1 onS. epidermidisRP62A biofilm formation. A) Growth control (not treated with SP1); B) sample treated with a sub-MIC concentration (3.1Â mg/ml) of SP1.
	Figure 7. Hemolytic activity of SP1 peptides fromParacentrotus lividushemocytes against rabbit blood cells at different concentrations: 1.5Â mg/ml; 3.2Â mg/ml; 6.2Â mg/ml; 50Â mg/ml. Data are the mean value of three separate experiments and expressed as percentage of hemolysisâ€‰Â±â€‰SD