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

Biao Cheng, Yang Li, Liang Ma, Zhuoyi Wang, Robert B. Petersen, Ling Zheng, Yuchen Chen, Kun Huang

Research output: Contribution to journalReview articlepeer-review

19 Scopus citations

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.

Original languageEnglish
Pages (from-to)1876-1888
Number of pages13
JournalBiochimica et Biophysica Acta - Biomembranes
Volume1860
Issue number9
DOIs
StatePublished - Sep 2018

Keywords

  • Amyloidogenic proteins
  • Biomembrane
  • Peptide to lipid ratio
  • Protein misfolding diseases
  • Therapy

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