Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
Interaction between synthetic amyloid-beta-peptide (1-40) and its aggregation inhibitors studied by electrospray ionization mass spectrometry
Autore:
Skribanek, Z; Balaspiri, L; Mak, M;
Indirizzi:
Gedeon Richter Chem Works Ltd, H-1475 Budapest 10, Hungary Gedeon Richter Chem Works Ltd Budapest Hungary 10 5 Budapest 10, Hungary Univ Szeged, Dept Med Chem, H-6720 Szeged, Hungary Univ Szeged Szeged Hungary H-6720 Dept Med Chem, H-6720 Szeged, Hungary
Titolo Testata:
JOURNAL OF MASS SPECTROMETRY
fascicolo: 11, volume: 36, anno: 2001,
pagine: 1226 - 1229
SICI:
1076-5174(200111)36:11<1226:IBSA(A>2.0.ZU;2-Z
Fonte:
ISI
Lingua:
ENG
Soggetto:
ALZHEIMERS-DISEASE; SECONDARY STRUCTURE; PROTEIN;
Keywords:
amyloid-beta-peptide (1-40); melatonin; aggregation inhibitors; protein-ligand interactions; electrospray ionization mass spectrometry;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Physical, Chemical & Earth Sciences
Citazioni:
23
Recensione:
Indirizzi per estratti:
Indirizzo: Skribanek, Z Unitis Inc, Kinizsi U2-B, H-2040 Budaors, Hungary Unitis Inc Kinizsi U2-B Budaors Hungary H-2040 aors, Hungary
Citazione:
Z. Skribanek et al., "Interaction between synthetic amyloid-beta-peptide (1-40) and its aggregation inhibitors studied by electrospray ionization mass spectrometry", J MASS SPEC, 36(11), 2001, pp. 1226-1229

Abstract

It is generally postulated that amyloid-beta -peptides play a central rolein the progressive neurodegeneration observed in Alzheimer's disease. Important pathological properties of these peptides, such as neurotoxicity and resistance to proteolytic degradation, depend on the ability of amyloid-beta -peptides to form beta -sheet structures and/or amyloid fibrils. Amyloid-beta -peptides are known to aggregate spontaneously in vitro with the formation of amyloid fibrils. The intervention on the amyloid-beta -peptides aggregation process can be envisaged as an approach to stopping or slowing theprogression of Alzheimer's disease. In the last few years a number of small molecules have been reported to interfere with the in vitro aggregation of amyloid-beta -peptides. Melatonin, a hormone recently found to protect neurons against amyloid-beta -peptide toxicity, interacts with amyloid-beta -peptide (1-40) and amyloid-beta -peptide (1-42) and inhibits the progressive formation of beta -sheet and/or amyloid fibrils. These interactions between melatonin and the amyloid peptides have been demonstrated by circular dichroism (CD) and electron microscopy for amyloid-beta -peptide (1-40) and amyloid-beta -peptide (1-42) and by nuclear magnetic resonance (NMR) spectroscopy for amyloid-beta -peptide (1-40). Our electrospray ionization mass spectrometric (BSI-MS) studies also proved that there is a hydrophobic interaction between amyloid-beta -peptide (1-40) and melatonin and the proteolytic investigations suggested that the interaction took place on the 29-40 amyloid-beta -peptide segment. The wide-ranging application of these results would provide further information and help in biological research. Copyright(C) 2001 John Wiley & Sons, Ltd.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 09/04/20 alle ore 11:51:37