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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
Congo red
amyloid formation
electric field
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.
cris.lastimport.scopus | 2024-04-07T15:04:25Z | |
cris.lastimport.wos | 2024-04-10T00:56:07Z | |
dc.abstract.en | 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. | pl |
dc.affiliation | Wydział Chemii : Zakład Krystalochemii i Krystalofizyki | pl |
dc.affiliation | Wydział Lekarski : Zakład Bioinformatyki i Telemedycyny | pl |
dc.affiliation | Wydział Lekarski : Katedra Biochemii Lekarskiej | pl |
dc.affiliation | Wydział Lekarski : Zakład Chemii Fizjologicznej | pl |
dc.contributor.author | Stopa, Barbara - 133516 | pl |
dc.contributor.author | Piekarska, Barbara - 133138 | pl |
dc.contributor.author | Konieczny, Leszek | pl |
dc.contributor.author | Król, Marcin | pl |
dc.contributor.author | Rybarska, Janina | pl |
dc.contributor.author | Jagusiak, Anna - 129789 | pl |
dc.contributor.author | Spólnik, Paweł - 133465 | pl |
dc.contributor.author | Roterman-Konieczna, Irena - 133298 | pl |
dc.contributor.author | Urbanowicz, Barbara | pl |
dc.contributor.author | Piwowar, Piotr | pl |
dc.contributor.author | Lewiński, Krzysztof - 129948 | pl |
dc.date.accession | 2019-04-26 | pl |
dc.date.accessioned | 2019-04-08T11:27:40Z | |
dc.date.available | 2019-04-08T11:27:40Z | |
dc.date.issued | 2010 | pl |
dc.date.openaccess | 0 | |
dc.description.accesstime | w momencie opublikowania | |
dc.description.additional | Bibliogr. s. 48-50. Na publikacji autorka Roterman-Konieczna Irena podpisana jako Roterman Irena. | pl |
dc.description.number | 1 | pl |
dc.description.physical | 41-50 | pl |
dc.description.version | ostateczna wersja wydawcy | |
dc.description.volume | 8 | pl |
dc.identifier.doi | 10.2478/s11532-009-0107-y | pl |
dc.identifier.eissn | 1644-3624 | pl |
dc.identifier.issn | 1895-1066 | pl |
dc.identifier.project | ROD UJ / OP | pl |
dc.identifier.uri | https://ruj.uj.edu.pl/xmlui/handle/item/72518 | |
dc.identifier.weblink | https://www.degruyter.com/downloadpdf/j/chem.2010.8.issue-1/s11532-009-0107-y/s11532-009-0107-y.pdf | pl |
dc.language | eng | pl |
dc.language.container | eng | pl |
dc.rights | Udzielam licencji. Uznanie autorstwa - Użycie niekomercyjne - Bez utworów zależnych 3.0 Polska | * |
dc.rights.licence | CC-BY-NC-ND | |
dc.rights.uri | http://creativecommons.org/licenses/by-nc-nd/3.0/legalcode | * |
dc.share.type | otwarte czasopismo | |
dc.subject.en | Congo red | pl |
dc.subject.en | amyloid formation | pl |
dc.subject.en | electric field | pl |
dc.subtype | Article | pl |
dc.title | 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 | pl |
dc.title.journal | Central European Journal of Chemistry | pl |
dc.type | JournalArticle | pl |
dspace.entity.type | Publication |
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