Journal
MOLECULES
Volume 28, Issue 20, Pages -Publisher
MDPI
DOI: 10.3390/molecules28207080
Keywords
amyloid; aggregation; simulations; Alzheimer's disease; membrane
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The interactions between amyloid proteins and membranes have been extensively studied. Recent simulations have focused on the adsorption and insertion modes of amyloid-beta and tau proteins in membranes, aiming to design drugs that target the transient oligomers in Alzheimer's disease.
The interactions of amyloid proteins with membranes have been subject to many experimental and computational studies, as these interactions contribute in part to neurodegenerative diseases. In this review, we report on recent simulations that have focused on the adsorption and insertion modes of amyloid-beta and tau proteins in membranes. The atomistic-resolution characterization of the conformational changes of these amyloid proteins upon lipid cell membrane and free lipid interactions is of interest to rationally design drugs targeting transient oligomers in Alzheimer's disease.
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