Structural features affecting antimicrobial activity, membrane interaction and resistance to proteases of distinctin. (Articolo in rivista)

Type

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

Label

• Structural features affecting antimicrobial activity, membrane interaction and resistance to proteases of distinctin. (Articolo in rivista) (literal)

Anno

• 2008-01-01T00:00:00+01:00 (literal)

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

• 10.1021/bi800616k (literal)

Alternative label

• Dalla Serra M, Cirioni O, Vitale RM, Renzone G, Coraiola M, Giacometti A, Potrich C, Baroni E, Guella G, Sanseverino M, De Luca S, Scalise G, Amodeo P, Scaloni A. (2008)
  Structural features affecting antimicrobial activity, membrane interaction and resistance to proteases of distinctin.
  in Biochemistry (Easton)
  (literal)

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

• Dalla Serra M, Cirioni O, Vitale RM, Renzone G, Coraiola M, Giacometti A, Potrich C, Baroni E, Guella G, Sanseverino M, De Luca S, Scalise G, Amodeo P, Scaloni A. (literal)

Pagina inizio

• 7888 (literal)

Pagina fine

• 7899 (literal)

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

• 47 (literal)

Rivista

• Biochemistry (Rivista)

Note

• ISI Web of Science (WOS) (literal)

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

• ISPAAM, Prote & Mass Spectrometry Lab, Natl Res Council, I-80147 Naples, Italy CNR, Bruno Kessler Fdn, Inst Biophys, I-38100 Trento, Italy Polytech Marche Univ, Inst Infect Dis & Publ Hlth, I-60200 Ancona, Italy CNR, Inst Biomol Chem, I-80078 Pozzuoli Naples, Italy Univ Trent, Dept Phys, Bioorgan Chem Lab, I-38100 Trento, Italy Inbios Srl, I-80078 Naples, Italy CNR, Inst Biocstruct & Bioimages, I-80138 Naples, Italy (literal)

Titolo

• Structural features affecting antimicrobial activity, membrane interaction and resistance to proteases of distinctin. (literal)

Abstract

• The antimicrobial peptide distinctin consists of two peptide chains linked by a disulfide bridge; it presents a peculiar fold in water resulting from noncovalent dimerization of two heterodimeric molecules. To investigate the contribution of each peptide chain and the S-S bond to distinctin biochemical properties, different monomeric and homodimeric peptide analogues were synthesized and comparatively evaluated with respect to the native molecule. Our experiments demonstrate that the simultaneous occurrence of both peptide chains and the disulfide bond is essential for the formation of the quaternary structure of distinctin in aqueous media, able to resist protease action. In contrast, distinctin and monomeric and homodimeric analogues exhibited comparable antimicrobial activities, suggesting only a partial contribution of the S-S bond to peptide killing effectiveness. Relative bactericidal properties paralleled liposome permeabilization results, definitively demonstrating that microbial membranes are the main target of distinctin activity. Various biophysical experiments performed in membrane-mimicking media, before and after peptide addition, provided information about peptide secondary structure, lipid bilayer organization, and lipid-peptide orientation with respect to membrane surface. These data were instrumental in the generation of putative models of peptide-lipid supramolecular pore complexes. (literal)

Prodotto di

• Istituto di biofisica (IBF) (Istituto)
• Processi di membrana nella comunicazione intra- ed inter-cellulare (MD.P01.001.001) (Modulo)

Autore CNR

• MAURO DALLA SERRA (Unità di personale interno)

Incoming links:

Prodotto

• Istituto di biofisica (IBF) (Istituto)
• Processi di membrana nella comunicazione intra- ed inter-cellulare (MD.P01.001.001) (Modulo)

Autore CNR di

• MAURO DALLA SERRA (Unità di personale interno)

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

• Biochemistry (Rivista)