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

Misfolding of Amyloidogenic Proteins and Their Interactions with Membranes

1,2,†email, 1,3,†email and 1,†,* email
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)
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
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
PDF Full-text Download PDF Full-Text [873 KB, uploaded 27 December 2013 17:29 CET]

Export to BibTeX |

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