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Paracentrin 1, a synthetic antimicrobial peptide from the sea-urchin Paracentrotus lividus, interferes with staphylococcal and Pseudomonas aeruginosa biofilm formation
- Source :
- AMB Express
- Publication Year :
- 2014
- Publisher :
- Springer Verlag GMBH Germany, 2014.
-
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.
- Subjects :
- medicine.drug_class
AMP (Antimicrobial peptides)
Biofilm
Staphylococci
Pseudomonas aeruginosa
Paracentrotus lividus
Antibiotics
Antimicrobial peptides
Biophysics
Settore BIO/05 - Zoologia
Peptide
Biology
medicine.disease_cause
Settore BIO/19 - Microbiologia Generale
Applied Microbiology and Biotechnology
Microbiology
medicine
Mode of action
chemistry.chemical_classification
Antimicrobial
biology.organism_classification
chemistry
Settore CHIM/03 - Chimica Generale E Inorganica
Original Article
Subjects
Details
- Language :
- English
- Database :
- OpenAIRE
- Journal :
- AMB Express
- Accession number :
- edsair.doi.dedup.....ec16c13c2c409addfcaf4b4aca01ea6d