Anti-aggregating effect of the naturally occurring dipeptide carnosine on aβ1-42 fibril formation.

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. Car...

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Auteurs principaux:	Alessandra Aloisi, Amilcare Barca, Alessandro Romano, Sara Guerrieri, Carlo Storelli, Rosaria Rinaldi, Tiziano Verri
Format:	article
Langue:	EN
Publié:	Public Library of Science (PLoS) 2013
Sujets:	Medicine R Science Q
Accès en ligne:	https://doaj.org/article/619f70fcdc4745f8b1a9c1ea278c2ea1
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spelling	oai:doaj.org-article:619f70fcdc4745f8b1a9c1ea278c2ea12021-11-18T07:38:46ZAnti-aggregating effect of the naturally occurring dipeptide carnosine on aβ1-42 fibril formation.1932-620310.1371/journal.pone.0068159https://doaj.org/article/619f70fcdc4745f8b1a9c1ea278c2ea12013-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/23844165/?tool=EBIhttps://doaj.org/toc/1932-6203Carnosine 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 Aβ1-42, a major hallmark of AD injury. Atomic force microscopy and thioflavin T assays showed inhibition of Aβ1-42 fibrillogenesis in vitro and differences in the aggregation state of Aβ1-42 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/Aβ1-42 interactions. Overall, our results suggest an effective role of carnosine against Aβ1-42 aggregation.Alessandra AloisiAmilcare BarcaAlessandro RomanoSara GuerrieriCarlo StorelliRosaria RinaldiTiziano VerriPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 8, Iss 7, p e68159 (2013)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Alessandra Aloisi Amilcare Barca Alessandro Romano Sara Guerrieri Carlo Storelli Rosaria Rinaldi Tiziano Verri Anti-aggregating effect of the naturally occurring dipeptide carnosine on aβ1-42 fibril formation.
description	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 Aβ1-42, a major hallmark of AD injury. Atomic force microscopy and thioflavin T assays showed inhibition of Aβ1-42 fibrillogenesis in vitro and differences in the aggregation state of Aβ1-42 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/Aβ1-42 interactions. Overall, our results suggest an effective role of carnosine against Aβ1-42 aggregation.
format	article
author	Alessandra Aloisi Amilcare Barca Alessandro Romano Sara Guerrieri Carlo Storelli Rosaria Rinaldi Tiziano Verri
author_facet	Alessandra Aloisi Amilcare Barca Alessandro Romano Sara Guerrieri Carlo Storelli Rosaria Rinaldi Tiziano Verri
author_sort	Alessandra Aloisi
title	Anti-aggregating effect of the naturally occurring dipeptide carnosine on aβ1-42 fibril formation.
title_short	Anti-aggregating effect of the naturally occurring dipeptide carnosine on aβ1-42 fibril formation.
title_full	Anti-aggregating effect of the naturally occurring dipeptide carnosine on aβ1-42 fibril formation.
title_fullStr	Anti-aggregating effect of the naturally occurring dipeptide carnosine on aβ1-42 fibril formation.
title_full_unstemmed	Anti-aggregating effect of the naturally occurring dipeptide carnosine on aβ1-42 fibril formation.
title_sort	anti-aggregating effect of the naturally occurring dipeptide carnosine on aβ1-42 fibril formation.
publisher	Public Library of Science (PLoS)
publishDate	2013
url	https://doaj.org/article/619f70fcdc4745f8b1a9c1ea278c2ea1
work_keys_str_mv	AT alessandraaloisi antiaggregatingeffectofthenaturallyoccurringdipeptidecarnosineonab142fibrilformation AT amilcarebarca antiaggregatingeffectofthenaturallyoccurringdipeptidecarnosineonab142fibrilformation AT alessandroromano antiaggregatingeffectofthenaturallyoccurringdipeptidecarnosineonab142fibrilformation AT saraguerrieri antiaggregatingeffectofthenaturallyoccurringdipeptidecarnosineonab142fibrilformation AT carlostorelli antiaggregatingeffectofthenaturallyoccurringdipeptidecarnosineonab142fibrilformation AT rosariarinaldi antiaggregatingeffectofthenaturallyoccurringdipeptidecarnosineonab142fibrilformation AT tizianoverri antiaggregatingeffectofthenaturallyoccurringdipeptidecarnosineonab142fibrilformation
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Anti-aggregating effect of the naturally occurring dipeptide carnosine on aβ1-42 fibril formation.

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