Design and synthesis of new trehalose-conjugated pentapeptides as inhibitors of Aβ(1-42) fibrillogenesis and toxicity
| Autor: | Paolo De Bona, Filippo Caraci, Agata Copani, Bruno Pignataro, Maria Laura Giuffrida, Francesco Attanasio, Giuseppe Pappalardo, Enrico Rizzarelli, Sebastiano Cataldo |
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| Přispěvatelé: | DE BONA, P., GIUFFRIDA M., L., Caraci, F., Copani, A., Pignataro, B., Attanasio, F., Cataldo, S., Pappalardo, G., Rizzarelli, E. |
| Rok vydání: | 2009 |
| Předmět: |
Amyloid
Cell Survival Peptide Microscopy Atomic Force Biochemistry Mass Spectrometry chemistry.chemical_compound beta-sheet breaker peptide Structural Biology SFM mental disorders Drug Discovery Animals beta-sheet breaker peptides Molecular Biology Cells Cultured Chromatography High Pressure Liquid trehalose Cerebral Cortex Pharmacology chemistry.chemical_classification thioflavin T beta-amyloid Organic Chemistry P3 peptide Fibrillogenesis General Medicine Trehalose Small molecule Glycopeptide Neuronal cultures Rats Peptide Conformation neuronal culture chemistry Molecular Medicine Amyloid-beta Peptides |
| Zdroj: | Journal of peptide science (Online) 15 (2009): 220–228. doi:10.1002/psc.1109 info:cnr-pdr/source/autori:De Bona, P.; Giuffrida, M.L.; Caraci, F.; Copani, A.; Pignataro, B.; Attanasio, F.; Cataldo, S.; Pappalardo, G.; Rizzarelli, E./titolo:Design and synthesis of new trehalose-conjugated pentapeptides as inhibitors of A?(1-42) fibrillogenesis and toxicity/doi:10.1002%2Fpsc.1109/rivista:Journal of peptide science (Online)/anno:2009/pagina_da:220/pagina_a:228/intervallo_pagine:220–228/volume:15 |
| ISSN: | 1099-1387 1075-2617 |
| DOI: | 10.1002/psc.1109 |
| Popis: | 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 iA?5p,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. Copyright © 2009 European Peptide Society and John Wiley & Sons, Ltd. |
| Databáze: | OpenAIRE |
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