Exploring interactions between lipids and amyloid-forming proteins: A review on applying fluorescence and NMR techniques. (May 2021)

• Record Type: Journal Article
• Authors: Chang, Ziwei; Deng, Jing; Zhao, Weijing; Yang, Jun
• Is Part Of: Chemistry and physics of lipids. Volume 236(2021)
• Publication Date: 2021-05
• Subjects: Amyloid protein -- Lipid -- Fluorescence -- Solution NMR -- Solid-state NMR; Lipids -- Periodicals; Lipids -- Periodicals; Lipides -- Périodiques; Lipids; Periodicals; Electronic journals; 547.77
• DOI: 10.1016/j.chemphyslip.2021.105062
• Languages: English
• ISSNs: 0009-3084

Abstract

Highlights: Lipid membranes and amyloid proteins have a very close relation in amyloid disease and amyloid assemblies' cytotoxicity. Fluorescence methods enable high sensitivity detection in the complicated amyloid protein-lipid system. Abundant information at atomic resolution can be obtained by solution and solid-state NMR spectroscopy. Abstract: 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.