Structure, conformation and biological activity of a novel lipodepsipeptide from Pseudomonas corrugata: cormycin A1 (Articolo in rivista)

Type

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

Label

• Structure, conformation and biological activity of a novel lipodepsipeptide from Pseudomonas corrugata: cormycin A1 (Articolo in rivista) (literal)

Anno

• 2004-01-01T00:00:00+01:00 (literal)

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

• 10.1042/BJ20040422 (literal)

Alternative label

• Andrea SCALONI; Mauro DALLA SERRA; Pietro AMODEO; Luisa MANNINA; Rosa Maria VITALE; Anna Laura SEGRE; Oscar CRUCIANI; Francesca LODOVICHETTI; Maria Luigia GRECO; Alberto FIORE; Monica GALLO; Chiara D'AMBROSIO; Manuela CORAIOLA; Gianfranco MENESTRINA; Antonio GRANITI; Vincenzo FOGLIANO (2004)
  Structure, conformation and biological activity of a novel lipodepsipeptide from Pseudomonas corrugata: cormycin A1
  in Biochemical journal (Online)
  (literal)

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

• Andrea SCALONI; Mauro DALLA SERRA; Pietro AMODEO; Luisa MANNINA; Rosa Maria VITALE; Anna Laura SEGRE; Oscar CRUCIANI; Francesca LODOVICHETTI; Maria Luigia GRECO; Alberto FIORE; Monica GALLO; Chiara D'AMBROSIO; Manuela CORAIOLA; Gianfranco MENESTRINA; Antonio GRANITI; Vincenzo FOGLIANO (literal)

Pagina inizio

• 25 (literal)

Pagina fine

• 36 (literal)

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

• 384 (literal)

Rivista

• Biochemical journal (Rivista)

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

• 12 (literal)

Note

• ISI Web of Science (WOS) (literal)
• Scopu (literal)

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

• *Proteomics and Mass Spectrometry Laboratory, I.S.P.A.A.M., National Research Council, 80147 Naples, Italy, +ITC and Institute of Biophysics, National Research Council, 38050 Povo (Trento), Italy, ?Istituto di Chimica Biomolecolare, Consiglio Nazionale delle Ricerche, 80078 Pozzuoli (Naples), Italy, §Dipartimento di Scienze e Tecnologie Agroalimentari, Ambientali e Microbiologiche, Universit`a di Molise, 86100 Campobasso, Italy, ?Istituto di Biostrutture e Bioimmagini, Consiglio Nazionale delle Ricerche, 80134 Napoli, Italy, ¶Institute of Chemical Methodologies, National Research Council, 00016 Monterotondo Stazione (Rome), Italy, **Dipartimento di Biologia e Patologia Vegetale, Universit`a di Bari, 70126 Bari, Italy, and ++Dipartimento di Scienza degli Alimenti, Universit`a di Napoli \"Federico II\", Parco Gussone, Edificio 84, 80055 Portici (Naples), Italy (literal)

Titolo

• Structure, conformation and biological activity of a novel lipodepsipeptide from Pseudomonas corrugata: cormycin A1 (literal)

Abstract

• Cationic lipodepsipeptides from Pseudomonas spp. have been characterized for their structural and antimicrobial properties. In the present study, the structure of a novel lipodepsipeptide, cormycin A, produced in culture by the tomato pathogen Pseudomonas corrugata was elucidated by combined protein chemistry, mass spectrometry and two-dimensional NMR procedures. Its peptide moiety corresponds to L-Ser-D-Orn-L-Asn-D-Hse-L-His- L-aThr-Z-Dhb-L-Asp(3-OH)-L-Thr(4-Cl) [where Orn represents ornithine, Hse is homoserine, aThr is allo-threonine, Z-Dhb is 2,3- dehydro-2-aminobutanoic acid, Asp(3-OH) is 3-hydroxyaspartic acid and Thr(4-Cl) is 4-chlorothreonine], with the terminal carboxy group closing a macrocyclic ring with the hydroxy group of the N-terminal serine residue. This is, in turn, N-acylated by 3,4-dihydroxy-esadecanoate. In aqueous solution, cormycin A showed a rather compact structure, being derived from an inward orientation of some amino acid side chains and from the 'hairpinbent' conformation of the lipid, due to inter-residue interactions involving its terminal part. Cormycin was significantly more active than the other lipodepsipeptides from Pseudomonas spp., as demonstrated by phytotoxicity and antibiosis assays, as well as by red-blood-cell lysis. Differences in biological activity were putatively ascribed to its weak positive net charge at neutral pH. Planar lipid membrane experiments showed step-like current transitions, suggesting that cormycin is able to form pores. This ability was strongly influenced by the phospholipid composition of the membrane and, in particular, by the presence of sterols. All of these findings suggest that cormycin derivatives could find promising applications, either as antifungal compounds for topical use or as post-harvest biocontrol agents. (literal)

Prodotto di

• Institute of biostructure and bioimaging (IBB) (Istituto)
• Istituto di chimica biomolecolare (ICB) (Istituto)
• Institute for animal production system in mediterranean environment (ISPAAM) (Istituto)

Autore CNR

• ROSA MARIA VITALE (Persona)
• MAURO DALLA SERRA (Unità di personale interno)
• ANDREA SCALONI (Persona)
• PIETRO AMODEO (Persona)

Insieme di parole chiave

• Parole chiave di "Structure, conformation and biological activity of a novel lipodepsipeptide from Pseudomonas corrugata: cormycin A1" (Insieme di parole chiave)

Incoming links:

Autore CNR di

• PIETRO AMODEO (Persona)
• ANDREA SCALONI (Persona)
• ROSA MARIA VITALE (Persona)
• MAURO DALLA SERRA (Unità di personale interno)

Prodotto

• Institute of biostructure and bioimaging (IBB) (Istituto)
• Institute for animal production system in mediterranean environment (ISPAAM) (Istituto)
• Istituto di chimica biomolecolare (ICB) (Istituto)

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

• Biochemical journal (Rivista)

Insieme di parole chiave di

• Parole chiave di "Structure, conformation and biological activity of a novel lipodepsipeptide from Pseudomonas corrugata: cormycin A1" (Insieme di parole chiave)