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Dendrimer‐amyloid Aggregates Morphology and Cell Toxicity

Appelhans, D.; Benseny, N.; Klementieva, Oxana LU ; Bryszewska, M.; Klajnert, B. and Cladera, J. (2013) p.1-13
Abstract
Dendrimers are branched polymeric structures that have been shown to have a promising antiamyloidogenic potential by interfering with the polymerization process leading to the formation of the amyloid aggregates related to conformational diseases, such as Alzheimer's and prion diseases. It has been established that there is a relationship between the morphology of the amyloid aggregates and the amyloid peptides or proteins toxicity: fibrillar structures present low or no toxicity, whereas oligomeric species and amorphous aggregates, the so called granular non‐fibrillar aggregates (GNAs), are toxic to cells. When interacting with the amyloid peptide associated to the onset and development of Alzheimer's disease, dendrimers can either... (More)
Dendrimers are branched polymeric structures that have been shown to have a promising antiamyloidogenic potential by interfering with the polymerization process leading to the formation of the amyloid aggregates related to conformational diseases, such as Alzheimer's and prion diseases. It has been established that there is a relationship between the morphology of the amyloid aggregates and the amyloid peptides or proteins toxicity: fibrillar structures present low or no toxicity, whereas oligomeric species and amorphous aggregates, the so called granular non‐fibrillar aggregates (GNAs), are toxic to cells. When interacting with the amyloid peptide associated to the onset and development of Alzheimer's disease, dendrimers can either accelerate the formation of fibrillar structures or inhibit it. Inhibition however may mean promoting the formation of amorphous aggregates. We summarize in the present chapter the experimental evidence showing that when used in a way that favors the formation and clumping of fibrils, dendrimers (glycodendrimers in particular) can reduce amyloid toxicity. However the same glycodendrimers used under different conditions can generate toxic GNAs, an aggregated form that could represent a general morphological signature for amyloid toxicity. (Less)
Please use this url to cite or link to this publication:
author
publishing date
type
Chapter in Book/Report/Conference proceeding
publication status
published
subject
host publication
Dendrimers in Biomedical Applications
editor
Klajnert, Barbara; Peng, Ling; Cena, Valentin; ; and
pages
1 - 13
ISBN
978-1-84973-729-6
978-1-84973-611-4
DOI
10.1039/9781849737296-00001
language
English
LU publication?
no
id
6316c8c1-07f7-4721-949c-7f4a4f8fc7e8
date added to LUP
2018-12-18 08:59:11
date last changed
2018-12-19 04:00:49
@inbook{6316c8c1-07f7-4721-949c-7f4a4f8fc7e8,
  abstract     = {Dendrimers are branched polymeric structures that have been shown to have a promising antiamyloidogenic potential by interfering with the polymerization process leading to the formation of the amyloid aggregates related to conformational diseases, such as Alzheimer's and prion diseases. It has been established that there is a relationship between the morphology of the amyloid aggregates and the amyloid peptides or proteins toxicity: fibrillar structures present low or no toxicity, whereas oligomeric species and amorphous aggregates, the so called granular non‐fibrillar aggregates (GNAs), are toxic to cells. When interacting with the amyloid peptide associated to the onset and development of Alzheimer's disease, dendrimers can either accelerate the formation of fibrillar structures or inhibit it. Inhibition however may mean promoting the formation of amorphous aggregates. We summarize in the present chapter the experimental evidence showing that when used in a way that favors the formation and clumping of fibrils, dendrimers (glycodendrimers in particular) can reduce amyloid toxicity. However the same glycodendrimers used under different conditions can generate toxic GNAs, an aggregated form that could represent a general morphological signature for amyloid toxicity.},
  author       = {Appelhans, D. and Benseny, N. and Klementieva, Oxana and Bryszewska, M. and Klajnert, B. and Cladera, J.},
  editor       = {Klajnert, Barbara and Peng, Ling and Cena, Valentin},
  isbn         = { 978-1-84973-729-6},
  language     = {eng},
  pages        = {1--13},
  title        = {Dendrimer‐amyloid Aggregates Morphology and Cell Toxicity},
  url          = {http://dx.doi.org/10.1039/9781849737296-00001},
  year         = {2013},
}