Please use this identifier to cite or link to this item: http://doi.org/10.25358/openscience-4877
Authors: Endres, Kristina
Title: Amyloidogenic peptides in human neuro-degenerative diseases and in microorganisms : a sorrow shared is a sorrow halved?
Online publication date: 10-Jun-2020
Language: english
Abstract: The term “amyloid” refers to proteinaceous deposits of peptides that might be generated from larger precursor proteins e.g., by proteolysis. Common to these peptides is a stable cross-β dominated secondary structure which allows self-assembly, leading to insoluble oligomers and lastly to fibrils. These highly ordered protein aggregates have been, for a long time, mainly associated with human neurodegenerative diseases such as Alzheimer’s disease (Amyloid-β peptides). However, they also exert physiological functions such as in release of deposited hormones in human beings. In the light of the rediscovery of our microbial commensals as important companions in health and disease, the fact that microbes also possess amyloidogenic peptides is intriguing. Transmission of amyloids by iatrogenic means or by consumption of contaminated meat from diseased animals is a well-known fact. What if also our microbial commensals might drive human amyloidosis or suffer from our aggregated amyloids? Moreover, as the microbial amyloids are evolutionarily older, we might learn from these organisms how to cope with the sword of Damocles forged of endogenous, potentially toxic peptides. This review summarizes knowledge about the interplay between human amyloids involved in neurodegenerative diseases and microbial amyloids. Keywords: amyloid; Alzheimer’s disease; biofilm; neurodegeneration; microbiota; Parkinson’s disease
DDC: 610 Medizin
610 Medical sciences
Institution: Johannes Gutenberg-Universität Mainz
Department: FB 04 Medizin
Place: Mainz
DOI: http://doi.org/10.25358/openscience-4877
Version: Published version
Publication type: Zeitschriftenaufsatz
License: CC-BY
Information on rights of use: https://creativecommons.org/licenses/by/4.0/
Journal: Molecules
25
4
Pages or article number: Art. 925
Publisher: MDPI
Publisher place: Basel
Issue date: 2020
ISSN: 1420-3049
Publisher's URL: http://dx.doi.org/10.3390/molecules25040925
Appears in collections:JGU-Publikationen

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