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2003 | 50 | 4 | 1213-1227
Article title

The structure and protein binding of amyloid-specific dye reagents.

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EN
Abstracts
EN
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.
Publisher

Year
Volume
50
Issue
4
Pages
1213-1227
Physical description
Dates
published
2003
received
2003-05-12
revised
2003-08-28
accepted
2003-09-15
Contributors
author
  • Institute of Medical Biochemistry, Collegium Medicum, Jagiellonian University, Kraków, Poland
  • Institute of Medical Biochemistry, Collegium Medicum, Jagiellonian University, Kraków, Poland
  • Institute of Medical Biochemistry, Collegium Medicum, Jagiellonian University, Kraków, Poland
  • Institute of Medical Biochemistry, Collegium Medicum, Jagiellonian University, Kraków, Poland
  • Institute of Medical Biochemistry, Collegium Medicum, Jagiellonian University, Kraków, Poland
  • Institute of Medical Biochemistry, Collegium Medicum, Jagiellonian University, Kraków, Poland
  • Department of Bioinformatics and Telemedicine, Collegium Medicum, Jagiellonian University, Kraków, Poland
author
  • Department of Bioinformatics and Telemedicine, Collegium Medicum, Jagiellonian University, Kraków, Poland
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Document Type
Publication order reference
Identifiers
YADDA identifier
bwmeta1.element.bwnjournal-article-abpv50i4p1213kz
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