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    Wyświetlanie 1-2 z 2
    Tytuł:
    The structure and protein binding of amyloid-specific dye reagents.
    Autorzy:
    Stopa, Barbara
    Piekarska, Barbara
    Konieczny, Leszek
    Rybarska, Janina
    Spólnik, Paweł
    Zemanek, Grzegorz
    Roterman, Irena
    Król, Marcin
    Powiązania:
    https://bibliotekanauki.pl/articles/1043414.pdf
    Data publikacji:
    2003
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    dye-protein complexation
    supramolecularity
    immunoglobulin light chain
    amyloid
    Congo red
    Opis:
    The self-assembling tendency and protein complexation capability of dyes related to Congo red and also some dyes of different structure were compared to explain the mechanism of Congo red binding and the reason for its specific affinity for β-structure. Complexation with proteins was measured directly and expressed as the number of dye molecules bound to heat-aggregated IgG and to two light chains with different structural stability. Binding of dyes to rabbit antibodies was measured indirectly as the enhancement effect of the dye on immune complex formation. Self-assembling was tested using dynamic light scattering to measure the size of the supramolecular assemblies. In general the results show that the supramolecular form of a dye is the main factor determining its complexation capability. Dyes that in their compact supramolecular organization are ribbon-shaped may adhere to polypeptides of β-conformation due to the architectural compatibility in this unique structural form. The optimal fit in complexation seems to depend on two contradictory factors involving, on the one hand, the compactness of the non-covalently stabilized supramolecular ligand, and the dynamic character producing its plasticity on the other. As a result, the highest protein binding capability is shown by dyes with a moderate self-assembling tendency, while those arranging into either very rigid or very unstable supramolecular entities are less able to bind.
    Źródło:
    Acta Biochimica Polonica; 2003, 50, 4; 1213-1227
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
    Tytuł:
    Silver ions as em marker of congo red ligation sites in amyloids and amyloid-like aggregates
    Autorzy:
    Rybarska, Janina
    Konieczny, Leszek
    Jagusiak, Anna
    Chłopaś, Katarzyna
    Zemanek, Grzegorz
    Piekarska, Barbara
    Stopa, Barbara
    Piwowar, Piotr
    Woźnicka, Olga
    Roterman, Irena
    Powiązania:
    https://bibliotekanauki.pl/articles/1038701.pdf
    Data publikacji:
    2017
    Wydawca:
    Polskie Towarzystwo Biochemiczne
    Tematy:
    Congo red
    Titan yellow
    amyloids
    supramolecular dyes
    metal markers
    light chain
    amyloid-like aggregates
    edge loop
    Opis:
    Congo red (CR) is a known selective amyloid ligand. The focus of our work is identification (by EM imaging) of dye binding sites and their distribution in amyloids and amyloid-like aggregates formed in vitro. In order to produce the required contrast, CR has been indirectly combined with metal via including Titan yellow (TY) by intercalation which exhibits a relatively strong affinity for silver ions. The resulting combined ligand retains its ability to bind to proteins (which it owes to CR) and can easily be detected in EM studies thanks to TY. We have found, however, that in protein aggregates where unfolding is stabilized by aggregation and therefore is irreversible, TY alone may serve as both, the ligand and the metal carrier. The formation of ordered structures in amyloids was studied using IgG light chains with amyloidogenic properties, converted into amyloids by shaking. The resulting EM images were subjected to interpretation on the basis of the authors' earlier research on the CR/light chain complexation process. Our results indicate that dimeric light chains, which are the subject of our study, produce amyloids or amyloid-like complexes with chain-like properties and strong helicalization tendencies. Cursory analysis suggests that the edge polypeptide loops belonging to unstable light chains form intermolecular bridges which promote creation of loose gel deposits, or are otherwise engaged in the swapping processes leading to higher structural ordering.
    Źródło:
    Acta Biochimica Polonica; 2017, 64, 1; 161-169
    0001-527X
    Pojawia się w:
    Acta Biochimica Polonica
    Dostawca treści:
    Biblioteka Nauki
    Artykuł
      Wyświetlanie 1-2 z 2

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