Design and synthesis of new trehalose-conjugated pentapeptides as inhibitors of Aβ(1–42) fibrillogenesis and toxicity

Bruno Giuseppe Pignataro, Sebastiano Cataldo, Giuseppe Pappalardo, Paolo De Bona, Filippo Caraci, Francesco Attanasio, Agata Copani, Maria Laura Giuffrida, Enrico Rizzarelli

Risultato della ricerca: Articlepeer review

36 Citazioni (Scopus)

Abstract

Aggregation of the amyloid A peptide and its accumulation into insoluble deposits (plaques) are believed to be the main cause of neuronal dysfunction associated with Alzheimer's disease (AD); small molecules that can interfere with the A amyloid fibril formation are therefore of interest for a potential therapeutic strategy. Three new trehalose-conjugated peptides of the well known -sheet breaker peptide iA5p, were synthesized. The disaccharide was covalently attached to different sites of the LPFFD peptide chain, i.e. at the N-terminus, C-terminus or at the Asp side chain. CD spectroscopy in different solvents was used to assess changes in the peptide conformation of these compounds. The effects of these glycopeptides on the self-assembly and morphology of A aggregates were investigated by ThT fluorescence assay and dynamic Scanning Force Microscopy, respectively. All the synthesized compounds were tested as inhibitors of A toxicity toward pure cultures of rat cortical neurons
Lingua originaleEnglish
pagine (da-a)220-228
Numero di pagine9
RivistaJournal of Peptide Science
Volume15
Stato di pubblicazionePublished - 2009

All Science Journal Classification (ASJC) codes

  • Structural Biology
  • Biochemistry
  • Molecular Medicine
  • Molecular Biology
  • Pharmacology
  • Drug Discovery
  • Organic Chemistry

Fingerprint Entra nei temi di ricerca di 'Design and synthesis of new trehalose-conjugated pentapeptides as inhibitors of Aβ(1–42) fibrillogenesis and toxicity'. Insieme formano una fingerprint unica.

Cita questo