New research has identified a potential trigger for amyloid formation, which is associated with diseases like Alzheimer’s and Parkinson’s. A study conducted in Japan has revealed that high liquid flow rates, particularly from peristaltic pump action, can cause proteins prone to aggregation to start sticking together, leading to the formation of amyloid fibrils.
High Flow Rates and Protein Clumping
Amyloidosis, the underlying cause of several severe diseases, occurs when misfolded proteins cluster together into crystal-like structures known as amyloid fibrils. These fibrils form when proteins become highly concentrated, or supersaturated, in bodily fluids such as blood and cerebrospinal fluid.
To understand the role of fluid dynamics in amyloid formation, researchers examined a model amyloid-forming protein, hen egg white lysozyme, by running it through a peristaltic pump similar to those used in dialysis. The protein’s behavior was monitored using fluorescence detection to track amyloid formation during the pumping process.
The results were striking. The peristaltic pumping action effectively triggered amyloid formation in the hen egg white lysozyme, demonstrating that high flow rates could influence protein aggregation.
Implications for Human Disease
To further validate the findings, researchers tested other amyloid-forming proteins linked to human diseases, including alpha-synuclein, amyloid beta 1-40, and beta-2 microglobulin. These proteins also formed amyloids when subjected to the peristaltic pump system.
Further analysis revealed that the shear stress exerted by the pumping motion disrupted protein supersaturation, leading to amyloid formation. This suggests that similar forces within the human body—such as those present in blood circulation or cerebrospinal fluid flow—could potentially contribute to amyloid formation and disease progression.
Potential Impact on Medical Procedures
The findings raise concerns about the role of peristaltic pumps in medical treatments, particularly in dialysis and other procedures where fluids are mechanically circulated. If the shear flow forces generated by these pumps can trigger amyloid formation, medical professionals may need to reassess certain treatment methods to reduce potential risks.
Understanding how shear forces influence protein behavior could offer new insights into the early stages of amyloid formation, potentially leading to new strategies for prevention and treatment. As researchers continue to explore these dynamics, the study provides a crucial step toward unraveling the complex mechanisms behind amyloidosis and related diseases.
