Szczegóły publikacji
Opis bibliograficzny
Formation of amyloid-like aggregates through the attachment of protein molecules to a Congo red scaffolding framework ordered under the influence of an electric field / Barbara Stopa, Barbara Piekarska, Leszek Konieczny, Marcin Król, Janina Rybarska, Anna Jagusiak, Paweł Spólnik, Irena Roterman, Barbara Urbanowicz, Piotr PIWOWAR, Krzysztof Lewiński // Central European Journal of Chemistry ; ISSN 1895-1066. — 2010 — vol. 8 iss. 1, s. 41–50. — Bibliogr. s. 48–50, Abstr. — Publikacja dostępna online od: 2010-05-29
Autorzy (11)
- Stopa Barbara
- Konieczny Leszek
- Król Marcin
- Rybarska Janina
- Jagusiak Anna
- Spólnik Paweł
- Roterman-Konieczna Irena
- Urbanowicz Barbara
- AGHPiwowar Piotr
- Lewiński Krzysztof
Redaktor
- Piekarska Barbara
Słowa kluczowe
Dane bibliometryczne
| ID BaDAP | 56469 |
|---|---|
| Data dodania do BaDAP | 2011-01-27 |
| Tekst źródłowy | URL |
| DOI | 10.2478/s11532-009-0107-y |
| Rok publikacji | 2010 |
| Typ publikacji | artykuł w czasopiśmie |
| Otwarty dostęp |  |
| Czasopismo/seria | Central European Journal of Chemistry |
Abstract
This study describes a technique which makes it possible to introduce the amyloid-like order to protein aggregates by using the scaffolding framework built from supramolecular, fibrillar Congo red structures arranged in an electric field. The electric field was used not only to obtain a uniform orientation of the charged dye fibrils, but also to make the fibrils long, compact and rigid due to the delocalization of pi electrons, which favors ring stacking and, as a consequence, results in an increased tendency to self-assemble. The protein molecules (immunoglobulin L chain lambda, ferritin) attached to this easily adsorbing dye framework assume its ordered structure. The complex precipitating as plate-like fragments shows birefringence in polarized light. The parallel organization of fibrils can be observed with an electron microscope. The dye framework may be removed via reduction with sodium dithionite, leaving the aggregated protein molecules in the ordered state, as confirmed by X-ray diffraction studies.
