Synthesis and activity of fibrillogenesis peptide inhibitors related to the 17-21 beta-amyloid sequence (Articolo in rivista)

Type
Label
  • Synthesis and activity of fibrillogenesis peptide inhibitors related to the 17-21 beta-amyloid sequence (Articolo in rivista) (literal)
Anno
  • 2009-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1016/j.ejmech.2008.03.036 (literal)
Alternative label
  • Giordano Cesare; Masi Annalisa; Pizzini Aldo; Sansone Anna; Consalvi Valerio; Chiaraluce Roberta; Lucente Gino (2009)
    Synthesis and activity of fibrillogenesis peptide inhibitors related to the 17-21 beta-amyloid sequence
    in European journal of medicinal chemistry
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Giordano Cesare; Masi Annalisa; Pizzini Aldo; Sansone Anna; Consalvi Valerio; Chiaraluce Roberta; Lucente Gino (literal)
Pagina inizio
  • 179 (literal)
Pagina fine
  • 189 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 44 (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
  • 1 (literal)
Note
  • Scopu (literal)
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • Istituto di Chimica Biomolecolare del CNR, Università ''La Sapienza'', P.le A. Moro 5, 00185 Roma, Italy; Dipartimento di Studi Farmaceutici, Universita` ''La Sapienza'', P.le A. Moro 5, 00185 Roma, Italy; Dipartimento di Scienze Biochimiche, Università ''La Sapienza'', P.le A. Moro 5, 00185 Roma, Italy. (literal)
Titolo
  • Synthesis and activity of fibrillogenesis peptide inhibitors related to the 17-21 beta-amyloid sequence (literal)
Abstract
  • Peptide derivatives 1e5, incorporating synthetic non-proteinogenic amino acids, related to the b-amyloid 17e21 fragment of the amyloidogenic Ab1e40, and the N-protected decapeptide 6, corresponding to a dimeric sequence of the same fragment, have been synthesized. These compounds were designed by using Soto's pentapeptide AceLPFFDeNH2 (iAb5p) as lead compound. Their activity as inhibitors of fibrillogenesis and stability against enzymatic degradation have been determined. Compounds 1, 5 and 6 are potent inhibitors in comparison to the lead compound. Exposure to chymotrypsin of peptide derivatives 1e5, all containing unnatural amino acids, shows increased stability as compared with iAb5p and 6. Conformational properties of the new compounds have been determined by CD and FT-IR spectroscopies. (literal)
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