Abstract

The inhibition of amyloid formation is a promisingtherapeutic approach for the treatment of neurodegenerativediseases. Peptide-based inhibitors, which have widely beeninvestigated, are generally derived from original amyloid sequences.Most interesting, trehalose, a non-reducing disaccharide of ?-glucose, is effective in preventing the aggregation of numerousproteins. We have determined that the development of hybridcompounds may provide new molecules with improved propertiesthat might sinergically increase the potency of their single moieties.In this work, the ability of the C-terminal trehalose conjugated Ac-LPFFD-Th derivative to slow down the A? aggregation process wasinvestigated by means of different biophysical techniques, includingTh-T fluorescence, DLS, ESI-MS and NMR. Moreover, wedemonstrate that Ac-LPFFD-Th modifies the aggregation features ofA? and protects neurons from A? oligomers' toxic insult.

Autore Pugliese

• Saviano Michele

Tutti gli autori

• A. Sinopoli; A. Giuffrida; M.F. Tomasello; M.L. Giuffrida; M. Leone; F. Attanasio; F. Caraci; P. De Bona; I. Naletova; M. Saviano; A. Copani; G. Pappalardo;E. Rizzarelli

Titolo volume/Rivista

ChemBioChem

Anno di pubblicazione

2016

ISSN

1439-4227

ISBN

Non Disponibile

Numero di citazioni Wos

Nessuna citazione

Ultimo Aggiornamento Citazioni

Non Disponibile

Numero di citazioni Scopus

Non Disponibile

Ultimo Aggiornamento Citazioni

Non Disponibile

Settori ERC

Non Disponibile

Codici ASJC

Non Disponibile