scholarly journals A generic approach to decipher the mechanistic pathway of heterogeneous protein aggregation kinetics

2021 ◽  
Author(s):  
Baishakhi Tikader ◽  
Samir K. Maji ◽  
Sandip Kar
Keyword(s):  
Protein Aggregation ◽  
Generic Property ◽  
Aggregation Kinetics ◽  
Amyloid Formation ◽  
Mechanistic Pathway ◽  
Polypeptide Chains

Amyloid formation is a generic property of many protein/polypeptide chains.

scholarly journals Effect of spin labelling on the aggregation kinetics of yeast prion protein Ure2

2021 ◽  
Vol 8 (3) ◽  
Author(s):  
Emilie N. Liu ◽  
Giovanna Park ◽  
Junsuke Nohara ◽  
Zhefeng Guo
Keyword(s):  
Protein Aggregation ◽  
Amyloid Fibrils ◽  
Prion Diseases ◽  
Aggregation Kinetics ◽  
Amyloid Formation ◽  
Yeast Prion ◽  
Aggregation Rate ◽  
Rate Limiting Step ◽  
Wide Range ◽  
Spin Labelling

Amyloid formation is involved in a wide range of neurodegenerative diseases including Alzheimer's and prion diseases. Structural understanding of the amyloid is critical to delineate the mechanism of aggregation and its pathological spreading. Site-directed spin labelling has emerged as a powerful structural tool in the studies of amyloid structures and provided structural evidence for the parallel in-register β-sheet structure for a wide range of amyloid proteins. It is generally accepted that spin labelling does not disrupt the structure of the amyloid fibrils, the end product of protein aggregation. The effect on the rate of protein aggregation, however, has not been well characterized. Here, we employed a scanning mutagenesis approach to study the effect of spin labelling on the aggregation rate of 79 spin-labelled variants of the Ure2 prion domain. The aggregation of Ure2 protein is the basis of yeast prion [URE3]. We found that all spin-labelled Ure2 mutants aggregated within the experimental timeframe of 15 to 40 h. Among the 79 spin-labelled positions, only five residue sites (N23, N27, S33, I35 and G42) showed a dramatic delay in the aggregation rate as a result of spin labelling. These positions may be important for fibril nucleation, a rate-limiting step in aggregation. Importantly, spin labelling at most of the sites had a muted effect on Ure2 aggregation kinetics, showing a general tolerance of spin labelling in protein aggregation studies.

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.

Protein Aggregation: Kinetics versus Thermodynamics

2012 ◽  
Vol 116 (18) ◽  
pp. 5384-5390 ◽  
Author(s):  
Piero Ricchiuto ◽  
Andrey V. Brukhno ◽  
Stefan Auer
Keyword(s):  
Protein Aggregation ◽  
Aggregation Kinetics

Silk protein aggregation kinetics revealed by Rheo-IR

2014 ◽  
Vol 10 (2) ◽  
pp. 776-784 ◽  
Author(s):  
Maxime Boulet-Audet ◽  
Ann E. Terry ◽  
Fritz Vollrath ◽  
Chris Holland
Keyword(s):  
Protein Aggregation ◽  
Silk Protein ◽  
Aggregation Kinetics
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