Abstract

Carnosine is an endogenous dipeptide abundant in the central nervous system, where by acting as intracellular pH buffering molecule, Zn/Cu ion chelator, antioxidant and anti-crosslinking agent, it exerts a well-recognized multi-protective homeostatic function for neuronal and non-neuronal cells. Carnosine seems to counteract proteotoxicity and protein accumulation in neurodegenerative conditions, such as Alzheimer's Disease (AD). However, its direct impact on the dynamics of AD-related fibril formation remains uninvestigated. We considered the effects of carnosine on the formation of fibrils/aggregates of the amyloidogenic peptide fragment A beta 1-42, a major hallmark of AD injury. Atomic force microscopy and thioflavin T assays showed inhibition of A beta 1-42 fibrillogenesis in vitro and differences in the aggregation state of A beta 1-42 small pre-fibrillar structures (monomers and small oligomers) in the presence of carnosine. in silico molecular docking supported the experimental data, calculating possible conformational carnosine/A beta 1-42 interactions. Overall, our results suggest an effective role of carnosine against A beta 1-42 aggregation

Autore Pugliese

• Aloisi Alessandra

Tutti gli autori

• Aloisi A. ; Barca A. ; Romano A. ; Guerrieri S. ; Storelli C. ; Rinaldi R. ; Verri T.

Titolo volume/Rivista

PloS one

Anno di pubblicazione

2013

ISSN

1932-6203

ISBN

Non Disponibile

Numero di citazioni Wos

Nessuna citazione

Ultimo Aggiornamento Citazioni

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Numero di citazioni Scopus

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Ultimo Aggiornamento Citazioni

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Settori ERC

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Codici ASJC

Non Disponibile