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Infrared nanospectroscopy characterization of oligomeric and fibrillar aggregates during amyloid formation

Publications associées (70)

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"Switch peptides"

Lydiane Jeanine Saucède

Despite of considerable progress in the research at the interface of Chemistry, Biology and Medicine, neurodegenerative diseases affect more and more seriously our ageing population and remain a real therapeutic challenge for researcher. Nevertheless, adva ...

EPFL2006

Le concept switch-peptides

Karine Murat

Conformational transitions have found broad interest due to their impact on protein misfolding and self-assembly as key events leading to the development of neurodegenerative diseases. However, investigation of these dynamic events has been limited so far ...

EPFL2006

New methods for the investigation of RNA refolding by NMR spectroscopy

Philipp Wenter

A detailed characterization of the time scales and mechanisms by which RNA molecules change their folding structure upon binding of metabolites or during catalysis is important for the understanding of the different biological functions of RNA. The folding ...

EPFL2006

Exogenous induction of cerebral beta-amyloidogenesis is governed by agent and host

Peter Frey, Tristan Bolmont, Paolo Paganetti

Protein aggregation is an established pathogenic mechanism in Alzheimer's disease, but little is known about the initiation of this process in vivo. Intracerebral injection of dilute, amyloid-beta (A beta)-containing brain extracts from humans with Alzheim ...

2006

Switch-peptides as folding precursors in amyloid fibrillogenesis

Richard Alan Mimna, Sonia Dos Santos, Karine Murat, Lydiane Jeanine Saucède, Marie-Stéphanie Camus, Jérémy Bérard

Intramol. O,N-acyl migration reactions were used as structural switch (S-elements) from a depsipeptide bond contg., unfolded state (Soff) to an all-amide, native states (Son). Chem. or enzymically triggered acyl migrations allowed for the controlled induct ...

2006

The materials science of protein aggregation

Hilal Lashuel

Numerous human diseases are associated with conformational change and aggregation of proteins, including Alzheimer's, Parkinson's, prion diseases (such as mad cow disease), familial amyotrophic lateral sclerosis (ALS, or Lou Gehrig's disease), Huntington's ...

Materials Research Society2005

Switch peptides

Richard Alan Mimna

Aspects of conformational transitions, folding, and misfolding of peptides and proteins have recently taken center stage in various domains at the interface of chemistry, biology, and medicine because of their impact on protein misfolding diseases. Due to ...

EPFL2005

Membrane permeabilization: a common mechanism in protein-misfolding diseases

Hilal Lashuel

Protein aggregation--and, more specifically, amyloid fibril formation--has been implicated as a primary cause of neurodegeneration in Alzheimer's disease, Parkinson's disease, and related disorders, but the mechanism by which this process triggers neuronal ...

2005

Dissociation of amyloid fibrils of alpha-synuclein and transthyretin by pressure reveals their reversible nature and the formation of water-excluded cavities

Hilal Lashuel

Protein misfolding and aggregation have been linked to several human diseases, including Alzheimer's disease, Parkinson's disease, and systemic amyloidosis, by mechanisms that are not yet completely understood. The hallmark of most of these diseases is the ...

National Academy of Sciences2003

Abeta protofibrils possess a stable core structure resistant to hydrogen exchange

Hilal Lashuel

Protofibrils are transient structures observed during in vitro formation of mature amyloid fibrils and have been implicated as the toxic species responsible for cell dysfunction and neuronal loss in Alzheimer's disease (AD) and other protein aggregation di ...

American Chemical Society2003