Abstract

Amyloid beta peptide (AP) is a natural peptide, normally released into the cerebrospinal fluid (CSF), that plays a key role in Alzheimer’s disease. The conversion of the peptide from a native soluble form to a non-native and often insoluble form, such as small and large aggregates, protofibrils and fibrils of AP appears to be implicated in the pathogenesis of AD. Although the molecular mechanisms of AP neurotoxicity are not fully understood, a large body of data suggests that the primary target of amyloid peptides is the cell membrane of neurons, that may modulate the structural and functional conversion of AP into assemblies involved in pathological processes. In our study, we provide a systematic investigation of AP1-42’s ability to incorporate and form channel-like events in membranes of different lipid composition and focus on cholesterol and its oxidation products. We propose that cholesterol and its oxidation products can be considered neuroprotective factors because a) by favouring AP1-42 insertion into membranes, the fibrillation/clearance balance shifts toward clearance; b) by shifting channel selectivity toward anions, the membrane potential is moved far from the threshold of membrane excitability, thus decreasing the influx of calcium into the cell.

Autore Pugliese

• Meleleo Daniela Addolorata

Tutti gli autori

• MELELEO D.A.

Titolo volume/Rivista

Non Disponibile

Anno di pubblicazione

2013

ISSN

1573-6881

ISBN

Non Disponibile

Numero di citazioni Wos

5

Ultimo Aggiornamento Citazioni

Non Disponibile

Numero di citazioni Scopus

6

Ultimo Aggiornamento Citazioni

Non Disponibile

Settori ERC

Non Disponibile

Codici ASJC

Non Disponibile