Effects of hypericin on the structure and aggregation properties of beta-amyloid peptides (Articolo in rivista)

Type
Label
  • Effects of hypericin on the structure and aggregation properties of beta-amyloid peptides (Articolo in rivista) (literal)
Anno
  • 2010-01-01T00:00:00+01:00 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
  • 10.1007/s00249-010-0607-x (literal)
Alternative label
  • Bramanti, Emilia (2); Lenci, Francesco (1); Sgarbossa, Antonella (1) (2010)
    Effects of hypericin on the structure and aggregation properties of beta-amyloid peptides
    in European biophysics journal
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Bramanti, Emilia (2); Lenci, Francesco (1); Sgarbossa, Antonella (1) (literal)
Pagina inizio
  • 1493 (literal)
Pagina fine
  • 1501 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#url
  • http://puma.isti.cnr.it/linkres.php?resource=cnr.ibf/cnr.ibf.pi/2010-A0-006 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 39 (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#pagineTotali
  • 9 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo
  • 11 (literal)
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • (1) CNR-IBF, Pisa; (2) CNR-IPCF, Pisa (literal)
Titolo
  • Effects of hypericin on the structure and aggregation properties of beta-amyloid peptides (literal)
Abstract
  • We have determined the secondary structure of 1-40 beta-amyloid peptides by Fourier-transform infrared spectroscopy (FTIR) and characterized the peptide photophysical properties before and after self-assembly by using intrinsic tyrosine steady-state and time-resolved fluorescence. All measurements were performed in the presence and absence of hypericin (Hyp), an exogenous natural polycyclic pigment that has been shown to inhibit fibril formation and has also been used as a fluorescent probe. We monitored the time course of the aggregation process measuring 405 nm light diffusion at 90° and used thioflavin T to reveal the presence of fibrils. FTIR quantitative analysis evidenced a prevalent random conformation at t = 0 with and without Hyp. Fibrils showed a predominant parallel beta-sheet structure and a small percentage of alpha-helix. The results of fluorescence measurements showed that Hyp does significantly interact with peptides in beta-sheet conformation. In conclusion, hypericin does hinder the formation of fibrils, but the percentages of parallel beta-sheets were not significantly different from those found in samples not treated with Hyp. (literal)
Prodotto di
Autore CNR
Insieme di parole chiave

Incoming links:


Prodotto
Autore CNR di
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#rivistaDi
Insieme di parole chiave di
data.CNR.it