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The misfolding of neuronal peptides such as Aβ40/42 in Alzheimer’s disease and cellular prion protein in scrapie induce abnormal aggregation of the peptides in the brain. The seeding of peptides’ oligomers from monomers is the initial step to form molten-globule states before abnormal aggregation. Therefore, compounds targeting the step are useful to clarify the mechanisms underlying aggregation of the proteins and Vitamin D derivatives, which can interact with both Aβ40 and cellular prion protein; however they show different effects in the oligomerization step of the proteins. We discuss the different effects of Vitamin D2 and Vitamin D3 in the interaction with these peptides in brain.

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Vitamin D Affects Neuronal Peptides in Neurodegenerative Disease: Differences of V-D2 and V-D3 for Affinity to Amyloid-β and Scrapie Prion Protein In Vitro