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Cytotoxicity of albebetin oligomers depends on cross-beta-sheet formation.

Identifieur interne : 002D42 ( Main/Exploration ); précédent : 002D41; suivant : 002D43

Cytotoxicity of albebetin oligomers depends on cross-beta-sheet formation.

Auteurs : Vladimir Zamotin [Suède] ; Anna Gharibyan ; Natalia V. Gibanova ; Marika A. Lavrikova ; Dmitry A. Dolgikh ; Michail P. Kirpichnikov ; Irina A. Kostanyan ; Ludmilla A. Morozova-Roche

Source :

RBID : pubmed:16638570

Descripteurs français

English descriptors

Abstract

Prefibrillar cytotoxicity was suggested as a common amyloid characteristic. We showed two types of albebetin prefibrillar oligomers are formed during incubation at pH 7.3. Initial round-shaped oligomers consist of 10-15 molecules determined by atomic force microscopy, do not bind thioflavin-T and do not affect viability of granular neurons and SH-SY5Y cells. They are converted into ca. 30-40-mers possessing cross-beta-sheet and reducing viability of neuronal cells. Neither monomers nor fibrils possess cytotoxicity. We suggest that oligomeric size is important for stabilising cross-beta-sheet core critical for cytotoxicity. As albebetin was used as a carrier-protein for drug delivery, examination of amyloidogenicity is required prior polypeptide biomedical applications.

DOI: 10.1016/j.febslet.2006.03.074
PubMed: 16638570


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<div type="abstract" xml:lang="en">Prefibrillar cytotoxicity was suggested as a common amyloid characteristic. We showed two types of albebetin prefibrillar oligomers are formed during incubation at pH 7.3. Initial round-shaped oligomers consist of 10-15 molecules determined by atomic force microscopy, do not bind thioflavin-T and do not affect viability of granular neurons and SH-SY5Y cells. They are converted into ca. 30-40-mers possessing cross-beta-sheet and reducing viability of neuronal cells. Neither monomers nor fibrils possess cytotoxicity. We suggest that oligomeric size is important for stabilising cross-beta-sheet core critical for cytotoxicity. As albebetin was used as a carrier-protein for drug delivery, examination of amyloidogenicity is required prior polypeptide biomedical applications.</div>
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