A folding-dependent mechanism of antimicrobial peptide resistance to degradation unveiled by solution structure of distinctin (Articolo in rivista)

Type

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

Label

• A folding-dependent mechanism of antimicrobial peptide resistance to degradation unveiled by solution structure of distinctin (Articolo in rivista) (literal)

Anno

• 2005-01-01T00:00:00+01:00 (literal)

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

• 10.1073/pnas.0409004102 (literal)

Alternative label

• Raimondo D.; Andreotti G.; Saint N.; Amodeo P.; Renzone G.; Sanseverino M.; Zocchi I.; Molle G.; Motta A.; Scaloni A. (2005)
  A folding-dependent mechanism of antimicrobial peptide resistance to degradation unveiled by solution structure of distinctin
  in Proceedings of the National Academy of Sciences of the United States of America
  (literal)

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

• Raimondo D.; Andreotti G.; Saint N.; Amodeo P.; Renzone G.; Sanseverino M.; Zocchi I.; Molle G.; Motta A.; Scaloni A. (literal)

Pagina inizio

• 6309 (literal)

Pagina fine

• 6314 (literal)

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

• 102 (literal)

Rivista

• Proceedings of the National Academy of Sciences of the United States of America (Rivista)

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

• 18 (literal)

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

• Viene descritto un nuovo meccanismo di \"autoprotezione\" dei peptidi privi di struttura tridimensionale. Mediante l'autoassociazione essi sono in grado di proteggersi dall'azione delle proteasi, inibendo così la degradazione. Quesdto meccanismo consente di progettare nuovi e potenti antibiotici contro ceppi betterici superresistenti. (literal)

Note

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

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

• Institute of Biomolecular Chemistry, National Research Council, Comprensorio Olivetti, Edificio 70, I-80078 Pozzuoli (Naples), Italy; Centre de Biochimie Structurale, Unité Mixte de Recherche 5048 Centre National de la Recherche Scientifique, U554 Institut National de la Santé et de la Recherche Médicale, F-34090 Montpellier, France; Proteomics and Mass Spectrometry Laboratory, Istituto per il Sistema Produzione Animale in Ambiente Mediterraneo (ISPAAM), National Research Council, I-80147 Naples, Italy; INBIOS S.r.l., Via Olivetti 1, I-80078 Pozzuoli (Naples), Italy. (literal)

Titolo

• A folding-dependent mechanism of antimicrobial peptide resistance to degradation unveiled by solution structure of distinctin (literal)

Abstract

• Many bioactive peptides, presenting an unstructured conformation in aqueous solution, are made resistant to degradation by posttranslational modifications. Here, we describe how molecular oligomerization in aqueous solution can generate a still unknown transport form for amphipathic peptides, which is more compact and resistant to proteases than forms related to any possible monomer. This phenomenon emerged from 3D structure, function, and degradation properties of distinctin, a heterodimeric antimicrobial compound consisting of two peptide chains linked by a disulfide bond. After homodimerization in water, this peptide exhibited a fold consisting of a symmetrical full-parallel four-helix bundle, with a well secluded hydrophobic core and exposed basic residues. This fold significantly stabilizes distinctin against proteases compared with other linear amphipathic peptides, without affecting its antimicrobial, hemolytic, and ion-channel formation properties after membrane interaction. This full-parallel helical orientation represents a perfect compromise between formation of a stable structure in water and requirement of a drastic structural rearrangement in membranes to elicit antimicrobial potential. Thus, distinctin can be claimed as a prototype of a previously unrecognized class of antimicrobial derivatives. These results suggest a critical revision of the role of peptide oligomerization whenever solubility or resistance to proteases is known to affect biological properties. (literal)

Prodotto di

• Institute for animal production system in mediterranean environment (ISPAAM) (Istituto)
• Metodologie genomiche e proteomiche applicate al sistema zootecnico ed agroindustriale (AG.P01.015.001) (Modulo)
• Istituto di chimica biomolecolare (ICB) (Istituto)

Autore CNR

• ANDREA MOTTA (Persona)
• GIUSEPPINA ANDREOTTI (Persona)
• PIETRO AMODEO (Persona)
• ANDREA SCALONI (Persona)

Insieme di parole chiave

• Keywords of "A folding-dependent mechanism of antimicrobial peptide resistance to degradation unveiled by solution structure of distinctin" (Insieme di parole chiave)

Incoming links:

Autore CNR di

• PIETRO AMODEO (Persona)
• ANDREA SCALONI (Persona)
• GIUSEPPINA ANDREOTTI (Persona)
• ANDREA MOTTA (Persona)

Prodotto

• Institute for animal production system in mediterranean environment (ISPAAM) (Istituto)
• Istituto di chimica biomolecolare (ICB) (Istituto)
• Metodologie genomiche e proteomiche applicate al sistema zootecnico ed agroindustriale (AG.P01.015.001) (Modulo)

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

• Proceedings of the National Academy of Sciences of the United States of America (Rivista)

Insieme di parole chiave di

• Keywords of "A folding-dependent mechanism of antimicrobial peptide resistance to degradation unveiled by solution structure of distinctin" (Insieme di parole chiave)