scholarly journals AggFluor: Fluorogenic Toolbox Enables Direct Visualization of the Multi-Step Protein Aggregation Process in Live Cells

2020 ◽  
Vol 142 (41) ◽  
pp. 17515-17523
Author(s):  
Charles H. Wolstenholme ◽  
Hang Hu ◽  
Songtao Ye ◽  
Brian E. Funk ◽  
Divya Jain ◽  
...  
Keyword(s):  
Protein Aggregation ◽  
Live Cells ◽  
Aggregation Process ◽  
Direct Visualization

scholarly journals When aggregation-induced emission meets protein aggregates

2021 ◽  
Author(s):  
Sicheng Tang ◽  
Songtao Ye ◽  
Xin Zhang
Keyword(s):  
Protein Aggregation ◽  
Protein Aggregates ◽  
Human Diseases ◽  
Diagnosis And Treatment ◽  
Live Cells ◽  
Future Application ◽  
Aggregation Process ◽  
Aggregation Induced Emission ◽  
Unmet Demand ◽  
Shed Light

There is an unmet demand for research tools to monitor the multistep protein aggregation process in live cells, a process that has been associated with a growing number of human diseases. Recently, AIEgens have been developed to directly monitor the entire protein aggregation process in test tubes and live cells. Future application of AIEgens is expected to shed light on both diagnosis and treatment of disease rooted in protein aggregation.

scholarly journals Valorization of Apple Peels through the Study of the Effects on the Amyloid Aggregation Process of κ-Casein

Molecules ◽  
2021 ◽  
Vol 26 (8) ◽  
pp. 2371
Author(s):  
Valeria Guarrasi ◽  
Giacoma Cinzia Rappa ◽  
Maria Assunta Costa ◽  
Fabio Librizzi ◽  
Marco Raimondo ◽  
...  
Keyword(s):  
Protein Aggregation ◽  
Environmental Sustainability ◽  
Bovine Milk ◽  
Amyloid Formation ◽  
Aggregation Process ◽  
Amyloid Aggregation ◽  
Social Challenges ◽  
Force Microscopy ◽  
Atomic Force ◽  
Apple Peels

Waste valorization represents one of the main social challenges when promoting a circular economy and environmental sustainability. Here, we evaluated the effect of the polyphenols extracted from apple peels, normally disposed of as waste, on the amyloid aggregation process of κ-casein from bovine milk, a well-used amyloidogenic model system. The effect of the apple peel extract on protein aggregation was examined using a thioflavin T fluorescence assay, Congo red binding assay, circular dichroism, light scattering, and atomic force microscopy. We found that the phenolic extract from the peel of apples of the cultivar “Fuji”, cultivated in Sicily (Caltavuturo, Italy), inhibited κ-casein fibril formation in a dose-dependent way. In particular, we found that the extract significantly reduced the protein aggregation rate and inhibited the secondary structure reorganization that accompanies κ-casein amyloid formation. Protein-aggregated species resulting from the incubation of κ-casein in the presence of polyphenols under amyloid aggregation conditions were reduced in number and different in morphology.

scholarly journals 4D Imaging of Protein Aggregation in Live Cells

10.3791/50083 ◽  
2013 ◽  
Author(s):  
Rachel Spokoini ◽  
Maya Shamir ◽  
Alma Keness ◽  
Daniel Kaganovich
Keyword(s):  
Protein Aggregation ◽  
Live Cells ◽  
4D Imaging

Characterization and real-time imaging of the FTLD-related protein aggregation induced by amyloidogenic peptides

2015 ◽  
Vol 51 (41) ◽  
pp. 8652-8655 ◽  
Author(s):  
Ruei-Yu He ◽  
Yi-Chen Huang ◽  
Chao-Wei Chiang ◽  
Yu-Ju Tsai ◽  
Ting-Juan Ye ◽  
...  
Keyword(s):  
Protein Aggregation ◽  
Real Time ◽  
Live Cells ◽  
Related Protein ◽  
Amyloid Fibers ◽  
Real Time Imaging ◽  
C Terminus ◽  
Amyloidogenic Peptides

Q/N- and G-rich polypeptides from the TDP-43 C-terminus formed amyloid fibers in vitro and induced the aggregation of the transfected TDP-43-EGFP in live cells.

Detecting protein aggregation and interaction in live cells: A guide to number and brightness

Methods ◽  
2018 ◽  
Vol 140-141 ◽  
pp. 172-177 ◽  
Author(s):  
Rory Nolan ◽  
Maro Iliopoulou ◽  
Luis Alvarez ◽  
Sergi Padilla-Parra
Keyword(s):  
Protein Aggregation ◽  
Live Cells

Nanoparticulate strategies for the treatment of polyglutamine diseases by halting the protein aggregation process

2017 ◽  
Vol 43 (6) ◽  
pp. 871-888 ◽  
Author(s):  
Oscar Escalona-Rayo ◽  
Paulina Fuentes-Vázquez ◽  
Gerardo Leyva-Gómez ◽  
Bulmaro Cisneros ◽  
Rafael Villalobos ◽  
...  
Keyword(s):  
Protein Aggregation ◽  
Aggregation Process ◽  
Polyglutamine Diseases

Evolutionary selection for protein aggregation

2012 ◽  
Vol 40 (5) ◽  
pp. 1032-1037 ◽  
Author(s):  
Natalia Sanchez de Groot ◽  
Marc Torrent ◽  
Anna Villar-Piqué ◽  
Benjamin Lang ◽  
Salvador Ventura ◽  
...  
Keyword(s):  
Protein Aggregation ◽  
Protein Interactions ◽  
Current Knowledge ◽  
Protein Aggregates ◽  
Cellular Systems ◽  
Aggregation Process ◽  
Loss Of Function ◽  
Protein Protein Interactions ◽  
Wide Range ◽  
Range Of Functions

Protein aggregation is being found to be associated with an increasing number of human diseases. Aggregation can lead to a loss of function (lack of active protein) or to a toxic gain of function (cytotoxicity associated with protein aggregates). Although potentially harmful, protein sequences predisposed to aggregation seem to be ubiquitous in all kingdoms of life, which suggests an evolutionary advantage to having such segments in polypeptide sequences. In fact, aggregation-prone segments are essential for protein folding and for mediating certain protein–protein interactions. Moreover, cells use protein aggregates for a wide range of functions. Against this background, life has adapted to tolerate the presence of potentially dangerous aggregation-prone sequences by constraining and counteracting the aggregation process. In the present review, we summarize the current knowledge of the advantages associated with aggregation-prone stretches in proteomes and the strategies that cellular systems have developed to control the aggregation process.

In cellulo protein labelling with Ru-conjugate for luminescence imaging and bioorthogonal photocatalysis

2015 ◽  
Vol 51 (93) ◽  
pp. 16664-16666 ◽  
Author(s):  
Kalyan K. Sadhu ◽  
E. Lindberg ◽  
N. Winssinger
Keyword(s):  
Ruthenium Complex ◽  
Photocatalytic Reduction ◽  
Live Cells ◽  
Direct Visualization ◽  
Protein Labelling ◽  
Aryl Azide ◽  
Luminescence Imaging

Labelling of proteins with a luminescent ruthenium complex enables the direct visualization and photocatalytic reduction of aryl azide in live cells.

In-line characterization of a whey protein aggregation process: Aggregates size and rheological measurements

2013 ◽  
Vol 115 (1) ◽  
pp. 73-82 ◽  
Author(s):  
Fatou Toutie Ndoye ◽  
Nicolas Erabit ◽  
Denis Flick ◽  
Graciela Alvarez
Keyword(s):  
Protein Aggregation ◽  
Whey Protein ◽  
Aggregation Process ◽  
Rheological Measurements
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