Alzheimer’s disease (AD) has become the most common neurodegenerative disease. The
deposition of amyloid fibrils in the brain is one of the characteristics of AD. The fibrils are composed
of amyloid-β peptide (Aβ). Aβ is produced through a series event of protease cleavage of a transmembrane
protein called β-amyloid precursor protein (APP) which is commonly expressed in the
brain. The production of Aβ and its propensity to aggregation to form oligomers and fibrils are believed
to initiate a sequence of events that lead to AD dementia. The production of Aβ is influenced
by the transmembrane domain (TM) structure of APP. The structure variety of different Aβ assemblies
including oligomers and fibrils may result in different neurotoxicity to the brain. Therefore,
enormous work has been carried out to study the structure of APP TM and various Aβ assemblies.
Solid-state NMR has advantages in studying immobile protein structures with large molecular
weight. In this review, solid-state NMR structure of APP TM and different Aβ assemblies will be
discussed, especially various Aβ amyloid fibril structures. This structural information greatly enhanced
our understanding in AD, providing fundamental knowledge that will help in finding a treatment
Keywords: Alzheimer's disease, amyloid precursor protein, amyloid-β peptide, amyloid fibrils, oligomers, solid-state NMR.
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