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

Schillaci, Domenico; Cusimano, Maria Grazia; Spinello, Angelo; Barone, Giampaolo; Russo, Debora; Vitale, María; Parrinello, Daniela; Arizza, Vincenzo

doi:10.1186/s13568-014-0078-z

Cited by 25 publications

(17 citation statements)

References 59 publications

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“…On the other hand, residue K 7 is in a random coil conformation in the first stable conformation, due to the position of this amino acid in the centre of the loop. Similar results were recently obtained with the analogue fragment, SP1, from sea-urchin (Schillaci et al 2014).…”

Section: Resultssupporting

confidence: 89%

“…Most of known AMPs, have a cationic amphiphilic alpha-helical structure and they are able to target the cytoplasmic membrane and to provoke cell death by osmotic shock (Di Luca et al 2014). As previously described, also the peptide SP1 from the sea urchin P.lividus has a hydrophobic region of three non polar residues and cationic and polar residues at both ends, which renders the peptide soluble in aqueous solution and provide a binding site for bacterial membranes (Schillaci et al 2014). These structural features differently from most AMPs, are designed as transmembrane mimetic models (Chan et al 2004;Liu and Deber 1998;Stark et al 2002).…”

Section: Discussionmentioning

confidence: 99%

“…We recently reported that the 5-kDa peptide fraction from the coelomocyte cytosol (5-CC) of the Paracentrotus lividus, the sea-urchin from Mediterranean sea showed antimicrobial and anti-biofilm activity against human common pathogens (Schillaci et al 2010a(Schillaci et al , 2014.…”

Section: Introductionmentioning

confidence: 99%

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A peptide from human β thymosin as a platform for the development of new anti-biofilm agents for Staphylococcus spp. and Pseudomonas aeruginosa

Schillaci

Spinello

Cusimano

et al. 2016

World J Microbiol Biotechnol

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Conventional antibiotics might fail in the treatment of biofilm-associated infections causing infection recurrence and chronicity. The search for antimicrobial peptides has been performed with the aim to discover novel anti-infective agents active on pathogens in both planktonic and biofilm associated forms. The fragment 9-19 of human thymosin β4 was studied through 1 μs MD simulation. Two main conformations of the peptide were detected, both constituted by a central hydrophobic core and by the presence of peripheral charged residues suggesting a possible mechanism of interaction with two models of biological membranes, related to eukaryotic or bacterial membrane respectively. In addition, the peptide was chemically synthesized and its antimicrobial activity was tested in vitro against planktonic and biofilm form of a group of reference strains of Staphylococcus spp. and one P. aeruginosa strain. The human thymosin β4 fragment EIEKFDKSKLK showed antibacterial activity against staphylococcal strains and Pseudomonas aeruginosa ATCC 15442 at concentrations from 12.5 to 6.2 mg/ml and inhibited biofilm formation at sub-inhibitory concentrations (3.1-0.75 mg/ml). The activity of the fragment in inhibiting biofilm formation, could be due to the conformations highlighted by the MD simulations, suggesting its interaction with the bacterial membrane. Human thymosin β4 fragment can be considered a promising lead compound to develop novel synthetic or recombinant derivatives with improved pharmaceutical potential.

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Section: Resultssupporting

confidence: 89%

Section: Discussionmentioning

confidence: 99%

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A peptide from human β thymosin as a platform for the development of new anti-biofilm agents for Staphylococcus spp. and Pseudomonas aeruginosa

Schillaci

Spinello

Cusimano

et al. 2016

World J Microbiol Biotechnol

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“…However, the molecular mechanism underlying Enterococcus resistance to L12 requires further investigation in future studies. The MIC of L12 against S. aureus was similar to traditional antibacterial drugs, and the antibacterial activity of L12 was comparable with other AMPs (22)(23)(24)(25). Furthermore, the MICs of L12 exhibited no correlation with resistance to the tested antibiotics, the strains resistant to more antibiotics were not more resistant to L12, which suggested that L12 may be used to treat infections caused by MRSA strains.…”

Section: Discussionmentioning

confidence: 83%

Effects of the antimicrobial peptide L12 against multidrug‑resistant Staphylococcus aureus

Dai

et al. 2019

Mol Med Report

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Methicillin-resistant Staphylococcus aureus (S. aureus; MRSA) is one of the most common bacterial pathogens and MRSA infections are characterized by high mortality rates. Antimicrobial peptides are considered one of the most promising drugs for the treatment of resistant strains of S. aureus. The present study aimed to examine the antimicrobial activity of L12 against numerous bacterial species using the broth microdilution method. Furthermore, the synergistic effect of L12 combined with various antibacterial drugs was tested, and its antibacterial mechanism was investigated by a checkerboard assay. The alterations in bacterial morphology were detected by electron microscopy, and biofilm formation and removal were tested by crystal violet staining. The present results suggested that L12 affected the growth of gram-positive strains, particularly S. aureus. Electron microscopy analysis suggested that L12 may target the cell membrane, and L12 increased the antibacterial activity of vancomycin and levofloxacin, exerting a synergistic effect. However, the minimal inhibitory concentrations (MICs) of L12 were not correlated with antibiotic resistance, the strains resistant to more antibiotics were not more resistant to L12. A sub-MIC of L12 was able to inhibit biofilm formation in a dose-dependent manner; however, concentrations of L12 ≤10 times the MIC were not sufficient to degrade previously formed biofilm. Collectively, the present study suggested that L12 may represent a novel potential therapeutic molecule for the treatment of S. aureus infections.

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“…In particular, we focused on the smallest 11 amino acid peptide (9–19), whose molecular weight was 1251.7, that we called Paracentrin 1 (SP1, EVASFDKSKLK). We demonstrated a broad range of activity against planktonic and biofilm forms of representative pathogens, like staphylococcal strains and P. aeruginosa, but we found Minimum Inhibitory Concentration (IC)values in the order of mg/mL [ 10 ]. Subsequently, we compared the amino acid sequence of SP1 with the corresponding fragment 9–19 (EIEKFDKSKLK) of human thymosin β4 (Tβ4).…”

Section: Introductionmentioning

confidence: 99%

Antimicrobial and Antibiofilm Activity of a Recombinant Fragment of β-Thymosin of Sea Urchin Paracentrotus lividus

et al. 2018

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With the aim to obtain new antimicrobials against important pathogens such as Staphylococcus aureus and Pseudomonas aeruginosa, we focused on antimicrobial peptides (AMPs) from Echinoderms. An example of such peptides is Paracentrin 1 (SP1), a chemically synthesised peptide fragment of a sea urchin thymosin. In the present paper, we report on the biological activity of a Paracentrin 1 derivative obtained by recombination. The recombinant paracentrin RP1, in comparison to the synthetic SP1, is 22 amino acids longer and it was considerably more active against the planktonic forms of S. aureus ATCC 25923 and P. aeruginosa ATCC 15442 at concentrations of 50 µg/mL. Moreover, it was able to inhibit biofilm formation of staphylococcal and P. aeruginosa strains at concentrations equal to 5.0 and 10.7 µg/mL, respectively. Molecular dynamics (MD) simulations allowed to rationalise the results of the experimental investigations, providing atomistic insights on the binding of RP1 toward models of mammalian and bacterial cell membranes. Overall, the results obtained point out that RP1 shows a remarkable preference for bacterial membranes, in excellent agreement with the antibacterial activity, highlighting the promising potential of using the tested peptide as a template for the development of novel antimicrobial agents.

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

Cited by 25 publications

References 59 publications

A peptide from human β thymosin as a platform for the development of new anti-biofilm agents for Staphylococcus spp. and Pseudomonas aeruginosa

A peptide from human β thymosin as a platform for the development of new anti-biofilm agents for Staphylococcus spp. and Pseudomonas aeruginosa

Effects of the antimicrobial peptide L12 against multidrug‑resistant Staphylococcus aureus

Antimicrobial and Antibiofilm Activity of a Recombinant Fragment of β-Thymosin of Sea Urchin Paracentrotus lividus

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