Publications associées à Thioflavin

Effects of sedimentation, microgravity, hydrodynamic mixing and air-water interface on alpha-synuclein amyloid formation

Giovanni Dietler, Giovanni Longo, Jiangtao Zhou, Francesco Simone Ruggeri

The formation of amyloid fibrils is a characterizing feature of a range of protein misfolding diseases, including Parkinson's disease. The propensity of native proteins to form such amyloid fibril, both in vitro and in vivo, is highly sensitive to the surr ...

2020

Oligomerization Profile of Human Transthyretin Variants with Distinct Amyloidogenicity

Bruno Emanuel Ferreira De Sousa Correia

One of the molecular hallmarks of amyloidoses is ordered protein aggregation involving the initial formation of soluble protein oligomers that eventually grow into insoluble fibrils. The identification and characterization of molecular species critical for ...

2020

The Clustering of mApoE Anti-Amyloidogenic Peptide on Nanoparticle Surface Does Not Alter Its Performance in Controlling Beta-Amyloid Aggregation

Francesco Stellacci, Paulo Henrique Jacob Silva

The deposition of amyloid-beta (A beta) plaques in the brain is a significant pathological signature of Alzheimer's disease, correlating with synaptic dysfunction and neurodegeneration. Several compounds, peptides, or drugs have been designed to redirect o ...

2020

Unraveling the complexity of amyloid polymorphism using gold nanoparticles and cryo-EM

Francesco Stellacci, Hilal Lashuel, Nadine Aït Bouziad, Paulo Henrique Jacob Silva, Anass Chiki, Zekiye Pelin Güven, Urszula Beata Cendrowska, Sophie Vieweg, Marie Mueller

Increasing evidence suggests that amyloid polymorphism gives rise to different strains of amyloids with distinct toxicities and pathology-spreading properties. Validating this hypothesis is challenging due to a lack of tools and methods that allow for the ...

National Academy of Sciences2020

An Intein-based Strategy for the Production of Tag-free Huntingtin Exon 1 Proteins Enables New Insights into the Polyglutamine Dependence of Httex1 Aggregation and Fibril Formation

Hilal Lashuel, Annalisa Ansaloni, Sophie Vieweg, John Blaine Warner IV

The first exon of the Huntingtin protein (Httex1) is one of the most actively studied Htt fragments because its overexpression in R6/2 transgenic mice has been shown to recapitulate several key features of Huntington disease. However, the majority of bioph ...

Amer Soc Biochemistry Molecular Biology Inc2016

A subcutaneous cellular implant for passive immunization against amyloid-beta reduces brain amyloid and tau pathologies

Patrick Aebischer, Bernard Schneider, Vanessa Laversenne, Aurélien Lathuilière, Marco Stampanoni

Passive immunization against toxic misfolded proteins could offer protection against neurodegenerative disease. LathuiliSre et al. report the development of a retrievable device to encapsulate cells secreting recombinant anti-amyloid-beta antibodies. When ...

Oxford Univ Press2016

Structural differences of amyloid-beta fibrils revealed by antibodies from phage display

Hilal Lashuel, Patrick Droste

Background: Beside neurofibrillary tangles, amyloid plaques are the major histological hallmarks of Alzheimer's disease (AD) being composed of aggregated fibrils of beta-amyloid (A beta). During the underlying fibrillogenic pathway, starting from a surplus ...

Biomed Central Ltd2015

The OPEP protein model: from single molecules, amyloid formation, crowding and hydrodynamics to DNA/RNA systems

Alessandro Barducci

The OPEP coarse-grained protein model has been applied to a wide range of applications since its first release 15 years ago. The model, which combines energetic and structural accuracy and chemical specificity, allows the study of single protein properties ...

Royal Society of Chemistry2014

Universal Behavior in the Mesoscale Properties of Amyloid Fibrils

Paolo De Los Rios, Salvatore Assenza, Raffaele Mezzenga

Amyloid fibrils are ubiquitous proteinaceous aggregates occurring in vivo and in vitro, with an invariant structural fingerprint at the molecular length scale. However, interpretation of their mesoscopic architectures is complicated by diverse observable p ...

2014

Nucleation Process of a Fibril Precursor in the C-Terminal Segment of Amyloid-beta

Fabio Pietrucci

By extended atomistic simulations in explicit solvent and bias-exchange metadynamics, we study the aggregation process of 18 chains of the C-terminal segment of amyloid-beta, an intrinsically disordered protein involved in Alzheimer's disease and prone to ...

Amer Physical Soc2013

Fluorine-18 labeling of three novel D-peptides by conjugation with N-succinimidyl-4-[F-18]fluorobenzoate and preliminary examination by postmortem whole-hemisphere human brain autoradiography

Andrea Pfeifer, Andreas Muhs

Introduction: beta-Amyloid (A beta) plaques and neurofibrillary tangles are the main characteristics of Alzheimer's disease (AD). Positron emission tomography (PET), a high-resolution, sensitive, and noninvasive imaging technique, has been widely utilized ...

2012

Development of a Small D-Enantiomeric Alzheimer's Amyloid-beta Binding Peptide Ligand for Future In Vivo Imaging Applications

Andrea Pfeifer, Andreas Muhs

Alzheimer's disease (AD) is a devastating disease affecting predominantly the aging population. One of the characteristic pathological hallmarks of AD are neuritic plaques, consisting of amyloid-beta peptide (A beta). While there has been some advancement ...

Public Library Science2012

Imaging brain amyloid deposition using grating-based differential phase contrast tomography

Patrick Aebischer, Jean-Charles Bensadoun, Peter Modregger, Marco Stampanoni

One of the core pathological features of Alzheimer's disease (AD) is the accumulation of amyloid plaques in the brain. Current efforts of medical imaging research aim at visualizing amyloid plaques in living patients in order to evaluate the progression of ...

Elsevier2012

Multidimensional View of Amyloid Fibril Nucleation in Atomistic Detail

Fabio Pietrucci

Starting from a disordered aggregate, we have simulated the formation of ordered amyloid-like beta structures in a system formed by 18 polyvaline chains in explicit solvent, employing molecular dynamics accelerated by bias-exchange metadynamics. We exploit ...

2012

Investigation of Biophysical Properties of Biomolecules by Means of Atomic Force Microscopy

Jae Sun Jeong

Biomolecules are the building blocks of living organisms and perform the most important functions in a biological process. The aim of biophysics is to understand the biological functions of biomolecules in terms of their structure: structure and function o ...

EPFL2012

EARLY-ONSET DYSFUNCTION OF RETROSPLENIAL CORTEX PRECEDES OVERT AMYLOID PLAQUE FORMATION IN Tg2576 MICE

Guillaume Poirier

A mouse model of amyloid pathology was used to first examine using a cross sectional design changes in retrosplenial cortex activity in transgenic mice aged 5, 11, 17, and 23 months. Attention focused on: (1) overt amyloid labeled with beta-amyloid((1-42)) ...

2011

The Gamma-Secretase-Mediated Proteolytic Processing of APP C-Terminal Fragments as a Therapeutic Target for Alzheimer's Disease

Jemila Houacine

Alzheimer's disease (AD) is a devastating neurodegenerative disorder which severely impairs cognitive functions by triggering neuronal cell death and synaptic loss, and finally leads the patients to death. Two main histopathological hallmarks can be found ...

EPFL2011

Nucleation Dependent Polymerization of Amyloid-ß (Aß) as an Important Determinant of Aß Amyloid Formation and Neurotoxicity : Implications for the Pathogenesis of Alzheimer's Disease and Design of Therapies

Mohammad Asad Jan Qureshi

Aggregation and fibril formation of amyloid-β (Aβ) peptides play a pivotal role in the pathogenesis of Alzheimer's disease (AD). Aβ peptides, principally comprising of 40 or 42 amino acid residues (Aβ40 and Aβ42), are produced by proteolytic processing of ...

EPFL2010

"Switch peptides" : conception et synthèse d'inhibiteurs ou destructeurs potentiels de fibrilles amyloïdes

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