Exploring interactions between lipids and amyloid-forming proteins: A review on applying fluorescence and NMR techniques

A hallmark of Alzheimer's, Parkinson's, and other amyloid diseases is the assembly of amyloid proteins into amyloid aggregates or fibrils. In many cases, the formation and cytotoxicity of amyloid assemblies are associated with their interaction with cell membranes. Despite studied for many years, the characterization of the interaction is challenged for reasons on the multiple aggregation states of amyloid-forming proteins, transient and weak interactions in the complex system. Although several strategies such as computation biology, spectroscopy, and imaging methods have been performed, there is an urgent need to detail the molecular mechanism in different time scales and high resolutions. This review highlighted the recent applications of fluorescence, solution and solid-state NMR in exploring the interactions between amyloid protein and membranes attributing to their advantages of high sensitivity and atomic resolution.

Automated summary

Alzheimer's, Parkinson's, and other amyloid diseases are characterized by the assembly of amyloid proteins into aggregates or fibrils. The interaction between amyloid assemblies and cell membranes is associated with their formation and cytotoxicity. Various methods have been employed to study this interaction, but there is an urgent need to understand the molecular mechanisms at different time scales and with high resolutions. The recent applications of fluorescence, solution and solid-state NMR have provided insights into these interactions due to their high sensitivity and atomic resolution capabilities.