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2017 | 64 | 1 | 161-169
Article title

Silver ions as em marker of congo red ligation sites in amyloids and amyloid-like aggregates

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Abstracts
EN
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.
Publisher

Year
Volume
64
Issue
1
Pages
161-169
Physical description
Dates
published
2017
received
2016-07-17
revised
2016-08-16
accepted
2016-09-05
(unknown)
2016-12-19
Contributors
  • Chair of Medical Biochemistry, Medical College - Jagiellonian University, Kraków, Poland
  • Chair of Medical Biochemistry, Medical College - Jagiellonian University, Kraków, Poland
author
  • Chair of Medical Biochemistry, Medical College - Jagiellonian University, Kraków, Poland
  • Chair of Medical Biochemistry, Medical College - Jagiellonian University, Kraków, Poland
  • Chair of Medical Biochemistry, Medical College - Jagiellonian University, Kraków, Poland
  • Chair of Medical Biochemistry, Medical College - Jagiellonian University, Kraków, Poland
author
  • Chair of Medical Biochemistry, Medical College - Jagiellonian University, Kraków, Poland
author
  • Department of Measurements and Electronics, AGH University of Science and Technology, Kraków, Poland
  • Department of Cell Biology Imaging, Faculty of Biology, Earth Sciences, Jagiellonian University, Kraków, Poland
  • Department of Bioinformatics and Telemedicine, Medical College - Jagiellonian University, Kraków, Poland
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Document Type
Publication order reference
Identifiers
YADDA identifier
bwmeta1.element.bwnjournal-article-abpv64p161kz
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