|
ИСТИНА |
Войти в систему Регистрация |
ИСТИНА ЦЭМИ РАН |
||
Study of interaction between trehalose conjugated beta sheet breaker peptide and amyloid beta(1-42) monomersтезисы доклада
- Авторы: Giuffrida A., Attanasio F., Naletova I., Muronetz V., Sinopoli A., Pappalardo G., Rizzarelli E.
- Сборник: XXIII National Congress of Analytical Chemistry
- Тезисы
- Год издания: 2012
- Место издания: Isola d’ Elba, Italy
- Аннотация: Amyloid β-peptides are involved in several neuropathological conditions such as Alzheimer’s disease (AD). Due to the cytotoxicity of the early intermediate soluble Aβ species it is important to direct the efforts towards the inhibition of initial steps of amyloid aggregation. Inhibiting Aβ self-oligomerization could, therefore, provide a useful approach to treating and controlling the pathogenic pathways underlying Alzheimer’s disease (AD). Probably, agents that target the molecular recognition process preceding the formation of early intermediates are the most valuable candidates. In our laboratory we have conjugated a trehalose moiety to the known β-sheet breakers pentapeptides LPFFD (1). Trehalose has received special interest because it has been found to be effective in the treatment of neurodegenerative diseases associated with peptide or protein aggregation (2). The glycosidic moiety was covalently linked to the C-terminus of the aminoacid sequence. This peptide showed an increased resistance to proteases (1). In this work we investigated the ability of the trehalose conjugated peptide to recognize and bind the monomeric form of Aβ(1-42). In this regard, we used several analytical techniques, including Analytical Ultracentrifugation (AUC), Dynamic Light Scattering (DLS) and fluorescence spectroscopy. Furthermore, we have carried out limited proteolysis experiments, which were analysed using ESI-MS, in the attempt of finding out the amino acid region involved in the recognition process.
- Добавил в систему: Налетова Ирина Николаевна