Structure-activity relations of myxinidin, an antibacterial peptide derived from the epidermal mucus of hagfish (Articolo in rivista)

Type

• Prodotto della ricerca (Classe)
• Articolo in rivista (Classe)

Label

• Structure-activity relations of myxinidin, an antibacterial peptide derived from the epidermal mucus of hagfish (Articolo in rivista) (literal)

Anno

• 2013-01-01T00:00:00+01:00 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi

• 10.1128/AAC.01341-13 (literal)

Alternative label

• Cantisani M.; Leone M.; Mignogna E.; Kampanaraki K.; Falanga A.; Morelli G.; Galdiero M.; Galdiero S. (2013)
  Structure-activity relations of myxinidin, an antibacterial peptide derived from the epidermal mucus of hagfish
  in Antimicrobial agents and chemotherapy (Print)
  (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori

• Cantisani M.; Leone M.; Mignogna E.; Kampanaraki K.; Falanga A.; Morelli G.; Galdiero M.; Galdiero S. (literal)

Pagina inizio

• 5665 (literal)

Pagina fine

• 5673 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#url

• http://www.scopus.com/inward/record.url?eid=2-s2.0-84885897528&partnerID=q2rCbXpz (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume

• 57 (literal)

Rivista

• Antimicrobial agents and chemotherapy (Rivista)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo

• 11 (literal)

Note

• Scopu (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni

• Department of Pharmacy, CIRPEB and DFM, University of Naples Federico II, Naples, Italy; Istituto di Biostrutture e Bioimmagini, CNR, Naples, Italy; Center for Advanced Materials for Health Care IIT CRIB, Istituto Italiano di Tecnologia, Naples, Italy; Department of Experimental Medicine, II University of Naples, Naples, Italy (literal)

Titolo

• Structure-activity relations of myxinidin, an antibacterial peptide derived from the epidermal mucus of hagfish (literal)

Abstract

• The structure-activity relations of myxinidin, a peptide derived from epidermal mucus of hagfish, Myxine glutinosa L., were investigated. Analysis of key residues allowed us to design new peptides with increased efficiency. Antimicrobial activity of native and modified peptides demonstrated the key role of uncharged residues in the sequence; the loss of these residues reduces almost entirely myxinidin antimicrobial activity, while insertion of arginine at charged and uncharged position increases antimicrobial activity compared with that of native myxinidin. Particularly, we designed a peptide capable of achieving a high inhibitory effect on bacterial growth. Experiments were conducted using both Gram-negative and Gram-positive bacteria. Nuclear magnetic resonance (NMR) studies showed that myxinidin is able to form an amphipathic ?-helical structure at the N terminus and a random coil region at the C terminus. Copyright © 2013, American Society for Microbiology. All Rights Reserved. (literal)

Prodotto di

• Determinazione della struttura tridimensionale di biomolecole complesse con tecniche spettroscopiche e cristallografiche (PM.P01.022.001) (Modulo)
• Institute of biostructure and bioimaging (IBB) (Istituto)

Autore CNR

• MARILISA LEONE (Persona)

Incoming links:

Prodotto

• Institute of biostructure and bioimaging (IBB) (Istituto)
• Determinazione della struttura tridimensionale di biomolecole complesse con tecniche spettroscopiche e cristallografiche (PM.P01.022.001) (Modulo)

Autore CNR di

• MARILISA LEONE (Persona)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#rivistaDi

• Antimicrobial agents and chemotherapy (Rivista)