Biomolecules 2014, 4(1), 20-55; doi:10.3390/biom4010020
Review

Misfolding of Amyloidogenic Proteins and Their Interactions with Membranes

1,2,†email, 1,3,†email and 1,†,* email
1 Department of Physics, University of Genoa, Genoa 16146, Italy 2 Research Centre on the Molecular Basis of Neurodegeneration, Florence 50134 Italy 3 Department of Chemistry, Saint Lawrence University, Canton, NY 13617, USA All authors contributed equally to this work.
* Author to whom correspondence should be addressed.
Received: 4 November 2013; in revised form: 13 December 2013 / Accepted: 17 December 2013 / Published: 27 December 2013
(This article belongs to the Special Issue Protein Folding and Misfolding)
PDF Full-text Download PDF Full-Text [873 KB, uploaded 27 December 2013 17:29 CET]
Abstract: In this paper, we discuss amyloidogenic proteins, their misfolding, resulting structures, and interactions with membranes, which lead to membrane damage and subsequent cell death. Many of these proteins are implicated in serious illnesses such as Alzheimer’s disease and Parkinson’s disease. Misfolding of amyloidogenic proteins leads to the formation of polymorphic oligomers and fibrils. Oligomeric aggregates are widely thought to be the toxic species, however, fibrils also play a role in membrane damage. We focus on the structure of these aggregates and their interactions with model membranes. Study of interactions of amlyoidogenic proteins with model and natural membranes has shown the importance of the lipid bilayer in protein misfolding and aggregation and has led to the development of several models for membrane permeabilization by the resulting amyloid aggregates. We discuss several of these models: formation of structured pores by misfolded amyloidogenic proteins, extraction of lipids, interactions with receptors in biological membranes, and membrane destabilization by amyloid aggregates perhaps analogous to that caused by antimicrobial peptides.
Keywords: amyloidogenic proteins; misfolding; amyloid aggregation; fibrillogenesis; membrane permeabilization; amyloid toxicity

Article Statistics

Load and display the download statistics.

Citations to this Article

Cite This Article

MDPI and ACS Style

Relini, A.; Marano, N.; Gliozzi, A. Misfolding of Amyloidogenic Proteins and Their Interactions with Membranes. Biomolecules 2014, 4, 20-55.

AMA Style

Relini A, Marano N, Gliozzi A. Misfolding of Amyloidogenic Proteins and Their Interactions with Membranes. Biomolecules. 2014; 4(1):20-55.

Chicago/Turabian Style

Relini, Annalisa; Marano, Nadia; Gliozzi, Alessandra. 2014. "Misfolding of Amyloidogenic Proteins and Their Interactions with Membranes." Biomolecules 4, no. 1: 20-55.

Biomolecules EISSN 2218-273X Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert