| Literature DB >> 29466701 |
Biao Cheng1, Yang Li2, Liang Ma2, Zhuoyi Wang2, Robert B Petersen3, Ling Zheng4, Yuchen Chen2, Kun Huang5.
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.Entities:
Keywords: Amyloidogenic proteins; Biomembrane; Peptide to lipid ratio; Protein misfolding diseases; Therapy
Year: 2018 PMID: 29466701 DOI: 10.1016/j.bbamem.2018.02.013
Source DB: PubMed Journal: Biochim Biophys Acta Biomembr ISSN: 0005-2736 Impact factor: 3.747