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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 - AMB Express (2014)

Bottom Line: 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.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.

View Article: PubMed Central - HTML - PubMed

Affiliation: Dip. STEBICEF, Università degli Studi di Palermo, Via Archirafi, Palermo, 32-90123, Italy.

ABSTRACT
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.

No MeSH data available.


Related in: MedlinePlus

Ramachandran plot showing the values of psi and phi angles assumed by residues 2–10 of SP1 between 150 and 250 ns of the MD simulation.
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Figure 3: Ramachandran plot showing the values of psi and phi angles assumed by residues 2–10 of SP1 between 150 and 250 ns of the MD simulation.

Mentions: To investigate SP1 in physiological conditions, we performed a MD simulation using the model represented in Figure 1. The in silico study provided a comprehensive picture of the dynamic equilibrium existing among the possible backbone conformations of the small oligopeptide. In fact, the root mean square deviations (RMSD) in Figure 2 show that the peptide conformation continuously and consistently changes during the 400 ns of simulation. Essentially all possible backbone conformations are assumed. However, interestingly, between 150 and 250 ns the structure is more stable and preserved, before becoming again flexible and random. To analyse this time region quantitatively, we have reported the Ramachandran plot in Figure 3 of snapshots sampled every 10 ns. This plot shows that in this time range the different residues assume preferential local conformations. In particular, residues 2, 3, 4 and 8 are in the beta sheet conformation, residues 5, 6 and 9 are in the left-handed helix conformation, residue 7 is in the alpha helix conformation, while residue 10 is in the beta sheet conformation and only sporadically in the alpha helix conformation. The corresponding structure is depicted in Figure 4. The results obtained allow us to confirm that polar and apolar residues are not segregated on opposing surfaces through the long axis of the oligopeptide. In this peculiar conformation, the one that most frequently occurs in the investigated simulation time, the peptide possesses a hydrophobic non-amphipathic core constituted by V2, A3, S4, F5 with a hydrophobic region placed between E1 and D6. These features confer to SP1 properties similar to the AMPs with hydrophobic core.


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 - AMB Express (2014)

Ramachandran plot showing the values of psi and phi angles assumed by residues 2–10 of SP1 between 150 and 250 ns of the MD simulation.
© Copyright Policy - open-access
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC4230904&req=5

Figure 3: Ramachandran plot showing the values of psi and phi angles assumed by residues 2–10 of SP1 between 150 and 250 ns of the MD simulation.
Mentions: To investigate SP1 in physiological conditions, we performed a MD simulation using the model represented in Figure 1. The in silico study provided a comprehensive picture of the dynamic equilibrium existing among the possible backbone conformations of the small oligopeptide. In fact, the root mean square deviations (RMSD) in Figure 2 show that the peptide conformation continuously and consistently changes during the 400 ns of simulation. Essentially all possible backbone conformations are assumed. However, interestingly, between 150 and 250 ns the structure is more stable and preserved, before becoming again flexible and random. To analyse this time region quantitatively, we have reported the Ramachandran plot in Figure 3 of snapshots sampled every 10 ns. This plot shows that in this time range the different residues assume preferential local conformations. In particular, residues 2, 3, 4 and 8 are in the beta sheet conformation, residues 5, 6 and 9 are in the left-handed helix conformation, residue 7 is in the alpha helix conformation, while residue 10 is in the beta sheet conformation and only sporadically in the alpha helix conformation. The corresponding structure is depicted in Figure 4. The results obtained allow us to confirm that polar and apolar residues are not segregated on opposing surfaces through the long axis of the oligopeptide. In this peculiar conformation, the one that most frequently occurs in the investigated simulation time, the peptide possesses a hydrophobic non-amphipathic core constituted by V2, A3, S4, F5 with a hydrophobic region placed between E1 and D6. These features confer to SP1 properties similar to the AMPs with hydrophobic core.

Bottom Line: 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.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.

View Article: PubMed Central - HTML - PubMed

Affiliation: Dip. STEBICEF, Università degli Studi di Palermo, Via Archirafi, Palermo, 32-90123, Italy.

ABSTRACT
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.

No MeSH data available.


Related in: MedlinePlus