Insight into Amyloid Formation Using Congo Red as the Electrochemical Probe

2011 ◽  
Vol 23 (12) ◽  
pp. 2753-2756 ◽  
Author(s):  
Anthony J. Veloso ◽  
Tiffiny Chan ◽  
Vinci Wing Sze Hung ◽  
Leayen Lam ◽  
Kagan Kerman
Keyword(s):  
Congo Red ◽  
Amyloid Formation ◽  
Electrochemical Probe ◽  
Insight Into

Mechanistic insight into the early stages of amyloid formation using an anuran peptide

2019 ◽  
Vol 111 (5) ◽  
Author(s):  
Sourav Ray ◽  
Stephanie Holden ◽  
Lisandra L. Martin ◽  
Ajay Singh Panwar
Keyword(s):  
Amyloid Formation ◽  
Early Stages ◽  
Mechanistic Insight ◽  
Insight Into

scholarly journals Suppression by polycyclic compounds of the conversion of human amylin into insoluble amyloid

2003 ◽  
Vol 374 (3) ◽  
pp. 779-784 ◽  
Author(s):  
Jacqueline F. AITKEN ◽  
Kerry M. LOOMES ◽  
Barbara KONARKOWSKA ◽  
Garth J. S. COOPER
Keyword(s):  
Acridine Orange ◽  
Congo Red ◽  
Type Ii Diabetes Mellitus ◽  
Significant Inhibition ◽  
Molar Ratio ◽  
Amyloid Formation ◽  
Islet Amyloid ◽  
Polycyclic Compounds ◽  
Molar Excess ◽  
Human Amylin

There is a significant correlation between the occurrence of pancreatic islet amyloid and β-cell failure in advanced type II diabetes mellitus. Islet amyloid is composed primarily of the fibrillar form of the pancreatic hormone, amylin. Using thioflavin-T fluorescence binding and radioprecipitation assays, we investigated whether or not a series of small tricyclic compounds, tetracycline or Congo Red could interfere with the conversion of synthetic human amylin into its insoluble amyloid form. Of the compounds investigated, incubation of human amylin with a 20-fold molar excess of either Congo Red or Acridine Orange resulted in significant inhibition in the rate of amyloid formation. With Congo Red, maximal inhibition effectively occurred at a 1:1 molar ratio or greater over human amylin, whereas inhibition by Acridine Orange was dose-dependent. A 20-fold molar excess of the compound tetracycline also decreased insoluble amyloid content after extended incubation periods of approx. 20 h. Amyloid fibril morphology in the presence of tetracycline, as measured by transmission electron microscopy, was characterized by short fragmented fibrils compared with the longer and denser appearance of fibrils formed by amylin alone. These findings show that polycyclic compounds can suppress the formation of amyloid by human amylin, providing support for an alternative approach to peptide-based strategies by which islet amyloid formation could be modulated.

Synthesis of hcp-Co and mixture of hcp/fcc-Co crystals: Insight into their Congo red removal ability

2014 ◽  
Vol 29 (8) ◽  
pp. 989-995 ◽  
Author(s):  
Lixia Wang ◽  
Lijun Zhao ◽  
Min Wang
Keyword(s):  
Congo Red ◽  
Image Position ◽  
Insight Into

Abstract

A mechanistic insight into the rapid and selective removal of Congo Red by an amide functionalised Zn(ii) coordination polymer

2020 ◽  
Vol 49 (37) ◽  
pp. 12970-12984
Author(s):  
Anup Paul ◽  
Kabita Das ◽  
Anirban Karmakar ◽  
M. Fátima C. Guedes da Silva ◽  
Armando J. L. Pombeiro
Keyword(s):  
Coordination Polymer ◽  
Congo Red ◽  
Selective Removal ◽  
Congo Red Dye ◽  
Mechanistic Insight ◽  
Red Dye ◽  
Insight Into

1D Zn(ii) CP 1 shows a selective removal of the Congo Red dye amongst various dyes.

scholarly journals Discerning amyloid network in plants

2021 ◽  
Author(s):  
Avinash Y.Gahane ◽  
Nabodita Sinha ◽  
Talat Zahra ◽  
Ashwani K.Thakur
Keyword(s):  
Congo Red ◽  
Storage Proteins ◽  
Compositional Analysis ◽  
Seed Storage ◽  
Seed Storage Proteins ◽  
Amyloid Formation ◽  
Functional Roles ◽  
Plant Seeds ◽  
Glutamine Repeat ◽  
Protein Rich

AbstractAmyloids are proteinaceous fibrillar structures and are known for their pathogenic and functional roles across the kingdoms. Besides proteinaceous deposits, amyloid-like structures are present in small metabolite assemblies and fibrillar hydrogels. Recent cryoelectron microscopy studies have shed light on the heterogeneous nature of the amyloid structures and their association with carbohydrate or lipid molecules, suggesting that amyloids are not exclusively proteinaceous. The association of amyloids with carbohydrates is further supported because the gold-standard dye of amyloid detection, Congo red, also binds to carbohydrates, probably due to similar stacking interactions. We name the association between amyloids, carbohydrates and other biomolecules as amyloid-network and propose that plants might contain such structures. Specifically, we hypothesize that cereal seeds containing glutamine-repeat-rich granules of storage proteins may have amyloid-like structures. This is because, polyQ repeats are associated with protein aggregation and amyloid formation in humans and are linked to multiple neurodegenerative conditions. Also seed storage proteins and seed cell wall proteins possess carbohydrate affinity. Thus, plant seeds might contain an intercalated network of proteins and carbohydrates, lending strength, stability and dynamics to these structures. In this paper, we show that, plant seeds have a mesh-like network that shows apple-green birefringence on staining with Congo red, a characteristic of amyloids. This congophilic network is more prominent in protein-rich seed sections of wheat and lentils, as compared to starch-rich compartments of potato. The findings suggest an amyloid network in the seeds and might be extended to other plant tissues. Further investigation with mass spectrometry and other techniques would detail the exact compositional analysis of these networks.

scholarly journals Novel Mechanistic Insight into the Molecular Basis of Amyloid Polymorphism and Secondary Nucleation during Amyloid Formation

2013 ◽  
Vol 425 (10) ◽  
pp. 1765-1781 ◽  
Author(s):  
Jae Sun Jeong ◽  
Annalisa Ansaloni ◽  
Raffaele Mezzenga ◽  
Hilal A. Lashuel ◽  
Giovanni Dietler
Keyword(s):  
Molecular Basis ◽  
Amyloid Formation ◽  
Secondary Nucleation ◽  
Mechanistic Insight ◽  
Insight Into

Insight into adsorption mechanism of Congo red dye onto Bombax Buonopozense bark Activated-carbon using Central composite design and DFT studies

2021 ◽  
Vol 23 ◽  
pp. 100977
Author(s):  
Youness Achour ◽  
Lahoucine Bahsis ◽  
El-Houssaine Ablouh ◽  
Hicham Yazid ◽  
My Rachid Laamari ◽  
...  
Keyword(s):  
Activated Carbon ◽  
Central Composite Design ◽  
Congo Red ◽  
Adsorption Mechanism ◽  
Dft Studies ◽  
Congo Red Dye ◽  
Red Dye ◽  
Central Composite ◽  
Insight Into

scholarly journals Recruitment of Class I Hydrophobins to the Air:Water Interface Initiates a Multi-step Process of Functional Amyloid Formation

2011 ◽  
Vol 286 (18) ◽  
pp. 15955-15963 ◽  
Author(s):  
Vanessa K. Morris ◽  
Qin Ren ◽  
Ingrid Macindoe ◽  
Ann H. Kwan ◽  
Nolene Byrne ◽  
...  
Keyword(s):  
Self Assembly ◽  
Structural Rearrangement ◽  
Class I ◽  
Amyloid Formation ◽  
Interface Properties ◽  
Functional Amyloid ◽  
Remarkable Case ◽  
Macromolecular Assembly ◽  
Insight Into

Class I fungal hydrophobins form amphipathic monolayers composed of amyloid rodlets. This is a remarkable case of functional amyloid formation in that a hydrophobic:hydrophilic interface is required to trigger the self-assembly of the proteins. The mechanism of rodlet formation and the role of the interface in this process have not been well understood. Here, we have studied the effect of a range of additives, including ionic liquids, alcohols, and detergents, on rodlet formation by two class I hydrophobins, EAS and DewA. Although the conformation of the hydrophobins in these different solutions is not altered, we observe that the rate of rodlet formation is slowed as the surface tension of the solution is decreased, regardless of the nature of the additive. These results suggest that interface properties are of critical importance for the recruitment, alignment, and structural rearrangement of the amphipathic hydrophobin monomers. This work gives insight into the forces that drive macromolecular assembly of this unique family of proteins and allows us to propose a three-stage model for the interface-driven formation of rodlets.

scholarly journals Congo Red and amyloids: history and relationship

2019 ◽  
Vol 39 (1) ◽  
Author(s):  
Elmira I. Yakupova ◽  
Liya G. Bobyleva ◽  
Ivan M. Vikhlyantsev ◽  
Alexander G. Bobylev
Keyword(s):  
Congo Red ◽  
Qualitative Method ◽  
Historical Review ◽  
Protein Aggregates ◽  
Scientific Data ◽  
Tissue Sections ◽  
In Vivo Analysis ◽  
Insight Into

AbstractStaining with Congo Red (CR) is a qualitative method used for the identification of amyloids in vitro and in tissue sections. However, the drawbacks and artefacts obtained when using this dye can be found both in vitro and in vivo. Analysis of scientific data from previous studies shows that CR staining alone is not sufficient for confirmation of the amyloid nature of protein aggregates in vitro or for diagnosis of amyloidosis in tissue sections. In the present paper, we describe the characteristics and limitations of other methods used for amyloid studies. Our historical review on the use of CR staining for amyloid studies may provide insight into the pitfalls and caveats related to this technique for researchers considering using this dye.

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