Structural features of distinctin affecting peptide biological and biochemical properties (Articolo in rivista)

Type
Label
  • Structural features of distinctin affecting peptide biological and biochemical properties (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 of distinctin affecting peptide biological and biochemical properties
    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
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
  • 30 (literal)
Note
  • ISI Web of Science (WOS) (literal)
  • Scopu (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • Bruno Kessler Foundation, Institute of Biophysics, National Research Council, 38100 PoVo (Trento), Italy, Institute of Infectious Diseases and Public Health, Polytechnic Marche UniVersity, 60200 Ancona, Italy, Institute of Biomolecular Chemistry, National Research Council, 80078 Pozzuoli (Naples), Italy, Proteomics and Mass Spectrometry Laboratory, ISPAAM, National Research Council, 80147 Naples, Italy, Laboratory of Bioorganic Chemistry, Department of Physics, UniVersity of Trento, 38100 PoVo (Trento), Italy, Inbios S.r.l., 80078 Pozzuoli (Naples), Italy, and Institute of Biostructures and Bioimages, National Research Council, 80138 Naples, Italy (literal)
Titolo
  • Structural features of distinctin affecting peptide biological and biochemical properties (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)
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