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Mar. Drugs 2018, 16(10), 366; https://doi.org/10.3390/md16100366

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

1
CNR-IOM-DEMOCRITOS c/o International School for Advanced Studies (SISSA), Via Bonomea 265, 34136 Trieste, Italy
2
Dipartimento di Scienze Biologiche, Chimiche e Farmaceutiche, Università di Palermo, Via Archirafi 18, 90123 Palermo, Italy
*
Author to whom correspondence should be addressed.
Received: 13 September 2018 / Revised: 25 September 2018 / Accepted: 29 September 2018 / Published: 2 October 2018
(This article belongs to the Special Issue New Strategies to Counteract Antibiotic Resistance Mechanisms)
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Abstract

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. View Full-Text
Keywords: AMP (antimicrobial peptides); biofilm; Staphylococcus aureus; Pseudomonas aeruginosa; thymosin; Paracentrotus lividus; molecular dynamics AMP (antimicrobial peptides); biofilm; Staphylococcus aureus; Pseudomonas aeruginosa; thymosin; Paracentrotus lividus; molecular dynamics
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited (CC BY 4.0).
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Spinello, A.; Cusimano, M.G.; Schillaci, D.; Inguglia, L.; Barone, G.; Arizza, V. Antimicrobial and Antibiofilm Activity of a Recombinant Fragment of β-Thymosin of Sea Urchin Paracentrotus lividus. Mar. Drugs 2018, 16, 366.

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