Peristaltic Flow Triggers Amyloid Protein Aggregation

A recent study published in npj Biosensing reveals critical insights into the mechanisms behind amyloid protein aggregation, a process linked to severe neurodegenerative diseases, such as Alzheimer’s and Parkinson’s disease. Researchers from Osaka University, led by Yuji Goto, discovered that the flow of liquid through a peristaltic pump can act as a triggering factor for the aggregation of amyloidogenic proteins.

Amyloidosis: A Growing Concern

Amyloidosis involves the formation of amyloid fibrils, which are abnormal clumps of misfolded proteins that can accumulate in various tissues and organs. This process is particularly troubling in the context of our aging population. Yuji Goto stated, “Amyloidosis is a serious concern in our aging society, as elderly individuals are more likely to develop these conditions.” A fundamental requirement for amyloid formation is supersaturation, which occurs when proteins are highly concentrated in fluids like blood or cerebrospinal fluid. Despite this knowledge, the specific triggers that induce aggregation in supersaturated conditions are not fully understood.

Study Methodology

To elucidate these mechanisms, the research team employed a model amyloidogenic protein, hen egg white lysozyme, which was processed through a peristaltic pump akin to those used in dialysis. Utilizing fluorescence detection techniques, the researchers monitored the progression of lysozyme in the pump system.

Key Findings

The study revealed that:

• The flow through the peristaltic pump significantly enhanced the formation of amyloid fibrils from hen egg white lysozyme.
• Further tests demonstrated that other amyloidogenic proteins, such as α-synuclein, amyloid β 1-40, and β2-microglobulin, also exhibited similar amyloid formation in the peristaltic pump system.
• The shear stress generated by the pump’s movement seems to disrupt protein supersaturation, thereby triggering amyloid fibril formation.

Implications for Medical Procedures

The findings of this study are particularly relevant as many medical procedures, including dialysis, utilize peristaltic pumps. This potentially places patients at risk for developing amyloidosis due to the shear forces exerted by pumping fluids through these systems.

“Our findings suggest that shear flow forces in various bodily fluids, such as blood and cerebrospinal fluid, could trigger amyloid formation,” states Goto.

Understanding the Mechanisms of Amyloid Formation

To further assess these mechanisms, the study included detailed numerical analyses of the shear stress induced by the motion of a contacting rotor within the pump system:

Future Directions

Understanding the effects of shear forces on protein supersaturation is crucial for clarifying the onset of amyloid aggregates. Potential avenues for future research include:

• Assessing how variations in pump design affect protein aggregation rates.
• Evaluating the impact of different amyloidogenic proteins in peristaltic flow settings.
• Developing strategies to mitigate the risks of amyloidosis in patients undergoing dialysis or similar procedures.

Conclusion

The study underscores the significance of mechanical factors in conjunction with biochemical conditions that favor amyloid formation. As our clinical practices increasingly incorporate technologies such as peristaltic pumping, there is a critical need for ongoing research to fully understand the implications of these findings for patient health.

References

Goto, Y. et al. (2025). Peristaltic pump-triggered amyloid formation suggests shear stresses are in vivo risks for amyloid nucleation. npj Biosensing. DOI: 10.1038/s44328-025-00027-0.

Retrieved from Medical Xpress