Interaction between amyloidogenic proteins and biomembranes in protein misfolding diseases: Mechanisms, contributors, and therapy

Biochimica Et Biophysica Acta. Biomembranes
Biao ChengKun Huang

Abstract

The toxic deposition of misfolded amyloidogenic proteins is associated with more than fifty protein misfolding diseases (PMDs), including Alzheimer's disease, Parkinson's disease and type 2 diabetes mellitus. Protein deposition is a multi-step process modulated by a variety of factors, in particular by membrane-protein interaction. The interaction results in permeabilization of biomembranes contributing to the cytotoxicity that leads to PMDs. Different biological and physiochemical factors, such as protein sequence, lipid composition, and chaperones, are known to affect the membrane-protein interaction. Here, we provide a comprehensive review of the mechanisms and contributing factors of the interaction between biomembranes and amyloidogenic proteins, and a summary of the therapeutic approaches to PMDs that target this interaction. This article is part of a Special Issue entitled: Protein Aggregation and Misfolding at the Cell Membrane Interface edited by Ayyalusamy Ramamoorthy.

Citations

Jan 12, 2019·British Journal of Pharmacology·Yang LiKun Huang
Feb 23, 2020·Acta Pharmaceutica Sinica. B·Yang WangHaopeng Sun
Dec 24, 2019·The Journal of Physical Chemistry. B·Yangang PanYuri L Lyubchenko
Feb 28, 2020·Journal of Chemical Information and Modeling·Huynh Minh HungSon Tung Ngo

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