Congo red fluorescence upon binding to macromolecules – a possible explanation for the enhanced intensity
-
Grzegorz Zemanek
,
Anna Jagusiak
Abstract
The present study attempts to explain the reason for the selective generation of an increase in intensity of Congo red (CR) fluorescence as an effect of the dye interacting with proteins and polysaccharides. This supramolecular dye, which creates ribbon-shaped micelles in aqueous solutions when excited with blue light (470 nm), presents low fluorescence with a maximum within the orange-red light range (approximately 600 nm). In the same conditions, CR-stained preparations of heat-denatured proteins, some native proteins (e.g. cell surface receptors) and cellulose show intense orange-red fluorescence when observed using a fluorescence microscope. The fluormetric measurements showed that the factors that cause the dissociation of the ribbon-shaped CR micelle – ethanol, urea, dimethyl sulfoxide (DMSO) and cholate – all contributed to a significant increase in the fluorescence intensity of the CR solutions. The fluorescence measurements of CR bound to the immunoglobulin light lambda (L λ) chain and soluble carboxymethyl cellulose (CMC) showed a fluorescence intensity which was many times higher. In the case of the denatured (65°C) immunoglobulin L λ chain, the fluorescence intensity significantly exceeded the values observed for the factors which break down the CR micelles. The dissociation of the ribbon-shaped micelles and the complexation of the monomeric CR form with polymers are two of the factors explaining the intense fluorescence of protein and polysaccharide preparations stained with CR.
Author contributions: All the authors have accepted responsibility for the entire content of this submitted manuscript and approved submission.
Research funding: None declared.
Employment or leadership: None declared.
Honorarium: None declared.
Competing interests: The funding organization(s) played no role in the study design; in the collection, analysis, and interpretation of data; in the writing of the report; or in the decision to submit the report for publication.
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©2017 Walter de Gruyter GmbH, Berlin/Boston
Articles in the same Issue
- Frontmatter
- Research Articles
- In silico study of the structure and function of Streptococcus mutans plasmidic proteins
- The variability of protein structure with respect to the hydrophobic core
- Congo red fluorescence upon binding to macromolecules – a possible explanation for the enhanced intensity
- Genetic traces of never born proteins
- Distributed storage and recall of sentences
- Extracting the symmetry of the human face from digital photographs
- Repository of 3D images for education and everyday clinical practice purposes
Articles in the same Issue
- Frontmatter
- Research Articles
- In silico study of the structure and function of Streptococcus mutans plasmidic proteins
- The variability of protein structure with respect to the hydrophobic core
- Congo red fluorescence upon binding to macromolecules – a possible explanation for the enhanced intensity
- Genetic traces of never born proteins
- Distributed storage and recall of sentences
- Extracting the symmetry of the human face from digital photographs
- Repository of 3D images for education and everyday clinical practice purposes
