Recent Computational Advances Regarding Amyloid-β and Tau Membrane Interactions in Alzheimer's Disease

被引:4
|
作者
Nguyen, Phuong H. [1 ]
Derreumaux, Philippe [1 ,2 ]
机构
[1] Univ Paris Cite, Inst Biol Physicochim, CNRS, UPR 9080,Lab Biochim Theor,Fdn Edmond Rothschild, 13 Rue Pierre & Marie Curie, F-75005 Paris, France
[2] Inst Univ France IUF, F-75005 Paris, France
来源
MOLECULES | 2023年 / 28卷 / 20期
关键词
amyloid; aggregation; simulations; Alzheimer's disease; membrane; A-BETA; CHOLESTEROL; PROTEIN; SIMULATIONS; PEPTIDES; MONOMER; FORMS;
D O I
10.3390/molecules28207080
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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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页数:13
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