Nutriovia

In a study published recently in NPJ biotessensageResearchers from the University of Osaka have revealed that high liquid flows could cause protein subject to aggregation to start staying together.

Amylosis is the basis of several serious illnesses, such as Alzheimer’s disease and Parkinson’s disease. This process implies the formation of amyloid fibrils, collections of the crystal type of poorly folded protein which come together when the proteins are highly concentrated (supersaturated) in liquids such as blood or cerebrospinal fluid.

“Amylosis is a serious concern in our aging society, because the elderly are more likely to develop these conditions,” said the main author of the Yuji Goto study. “Although studies have shown that supersaturation is a necessary condition for the formation of amyloid fibriles, the factors that really induce protein aggregation in supersaturated fluids remain vague.”

To remedy this, the researchers directed an amyloid protein model, the white egg egg lysozyme, through a peristaltic pump similar to that used for dialysis. They then used fluorescence detection to monitor the amyloid formation of the white lysozyme with chicken eggs because it was powered by the pump system.

“The results were very intriguing,” said Hirotsugu Ogi, principal author. “The flow through the peristaltic pump system has effectively triggered the formation of amyloids by the white egg egg lysozyme.”

Then, the researchers tested proteins forming amyloids associated with human diseases, including a-synuclein, the amyloid B 1-40 and B2-Microglobulin, and found that they also formed amyloids in the peristaltic pump system. Their calculations have shown that the shear stress on the liquid caused by the pumping movement mechanically broke the supersaturation to induce amyloid formation.

“Our results suggest that shear flow forces in various fluids in our body, such as bloody blood and liquid, could trigger the formation of amyloids,” said Goto.

Since certain medical procedures such as dialysis use peristaltic pumps, it may be another trigger for amyloidosis. Understanding the effects of shear forces on protein sunseaturation could clarify how amyloid aggregates are starting to form a nucleation and help develop treatment strategies.

In a study published recently in NPJ biotessensageResearchers from the University of Osaka have revealed that high liquid flows could cause protein subject to aggregation to start staying together.

Amylosis is the basis of several serious illnesses, such as Alzheimer’s disease and Parkinson’s disease. This process implies the formation of amyloid fibrils, collections of the crystal type of poorly folded protein which come together when the proteins are highly concentrated (supersaturated) in liquids such as blood or cerebrospinal fluid.

“Amylosis is a serious concern in our aging society, because the elderly are more likely to develop these conditions,” said the main author of the Yuji Goto study. “Although studies have shown that supersaturation is a necessary condition for the formation of amyloid fibriles, the factors that really induce protein aggregation in supersaturated fluids remain vague.”

To remedy this, the researchers directed an amyloid protein model, the white egg egg lysozyme, through a peristaltic pump similar to that used for dialysis. They then used fluorescence detection to monitor the amyloid formation of the white lysozyme with chicken eggs because it was powered by the pump system.

“The results were very intriguing,” said Hirotsugu Ogi, principal author. “The flow through the peristaltic pump system has effectively triggered the formation of amyloids by the white egg egg lysozyme.”

Then, the researchers tested proteins forming amyloids associated with human diseases, including a-synuclein, the amyloid B 1-40 and B2-Microglobulin, and found that they also formed amyloids in the peristaltic pump system. Their calculations have shown that the shear stress on the liquid caused by the pumping movement mechanically broke the supersaturation to induce amyloid formation.

“Our results suggest that shear flow forces in various fluids in our body, such as bloody blood and liquid, could trigger the formation of amyloids,” said Goto.

Since certain medical procedures such as dialysis use peristaltic pumps, it may be another trigger for amyloidosis. Understanding the effects of shear forces on protein sunseaturation could clarify how amyloid aggregates are starting to form a nucleation and help develop treatment strategies.

In a study published recently in NPJ biotessensageResearchers from the University of Osaka have revealed that high liquid flows could cause protein subject to aggregation to start staying together.

Amylosis is the basis of several serious illnesses, such as Alzheimer’s disease and Parkinson’s disease. This process implies the formation of amyloid fibrils, collections of the crystal type of poorly folded protein which come together when the proteins are highly concentrated (supersaturated) in liquids such as blood or cerebrospinal fluid.

“Amylosis is a serious concern in our aging society, because the elderly are more likely to develop these conditions,” said the main author of the Yuji Goto study. “Although studies have shown that supersaturation is a necessary condition for the formation of amyloid fibriles, the factors that really induce protein aggregation in supersaturated fluids remain vague.”

To remedy this, the researchers directed an amyloid protein model, the white egg egg lysozyme, through a peristaltic pump similar to that used for dialysis. They then used fluorescence detection to monitor the amyloid formation of the white lysozyme with chicken eggs because it was powered by the pump system.

“The results were very intriguing,” said Hirotsugu Ogi, principal author. “The flow through the peristaltic pump system has effectively triggered the formation of amyloids by the white egg egg lysozyme.”

Then, the researchers tested proteins forming amyloids associated with human diseases, including a-synuclein, the amyloid B 1-40 and B2-Microglobulin, and found that they also formed amyloids in the peristaltic pump system. Their calculations have shown that the shear stress on the liquid caused by the pumping movement mechanically broke the supersaturation to induce amyloid formation.

“Our results suggest that shear flow forces in various fluids in our body, such as bloody blood and liquid, could trigger the formation of amyloids,” said Goto.

Since certain medical procedures such as dialysis use peristaltic pumps, it may be another trigger for amyloidosis. Understanding the effects of shear forces on protein sunseaturation could clarify how amyloid aggregates are starting to form a nucleation and help develop treatment strategies.