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Structure of Crenezumab Complex with A beta Shows Loss of beta-Hairpin
Related publications (33)
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 ...
2020Nanoscale Characterization of Amyloid Fibrils and Biomacromolecules by Atomic Force Microscopy Approaches
This thesis focuses on the interdisciplinary biophysical research field, in which physical approaches are applied to study the biological phenomena. Specifically, the main object of the research in this thesis is to target biological species,especially the ...
EPFL2020Synthesis and structure-activity relationship of 2,6-disubstituted pyridine derivatives as inhibitors of beta-amyloid-42 aggregation
Andrea Pfeifer, Andreas Muhs, Paolo Paganetti
It is assumed that amyloid-beta aggregation is a crucial event in the pathogenesis of Alzheimer's disease. Novel 2,6-disubstituted pyridine derivatives were designed to interact with the beta-sheet conformation of A beta via donor-acceptor-donor hydrogen b ...
Pergamon-Elsevier Science Ltd2016Real-time Protein Aggregation Monitoring based on a Simultaneous Light Scattering Investigation and a Bloch Surface Wave-based Approach
Hans Peter Herzig, Elsie Barakat, Sara Santi
We present a study of the dynamics of protein aggregation using a Bloch surface wave (BSW) label-free sensing scheme. In a previous work, we demonstrated the ability to detect the early dynamic events of fibrillogenesis of amyloid beta-peptides (A beta), l ...
Spie-Int Soc Optical Engineering2015Infrared nanospectroscopy characterization of oligomeric and fibrillar aggregates during amyloid formation
Giovanni Dietler, Giovanni Longo, Francesco Simone Ruggeri, Ewelina Wioletta Lipiec
Amyloids are insoluble protein fibrillar aggregates. The importance of characterizing their aggregation has steadily increased because of their link to human diseases and material science applications. In particular, misfolding and aggregation of the Josep ...
Nature Publishing Group2015New Insights Into Amyloid Formation and Structure by Innovative Atomic Force Microscopy Methods
Today, more than 40 million people worldwide are affected by neurodegenerative disorders. Onset of these diseases is associated with insoluble fibrillar protein aggregates, termed amyloids. The molecular origin and the link between amyloid formation and di ...
EPFL2015Structural differences of amyloid-beta fibrils revealed by antibodies from phage display
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 Ltd2015The centriolar protein CPAP G-box: an amyloid fibril in a single domain
Centrioles are evolutionarily conserved cylindrical cell organelleswith characteristic radial symmetry. Despite their considerable size (400 nm x 200 nm, in humans), genetic studies suggest that relatively few protein components are involved in their assem ...
Portland Press Ltd2015Influence of the β-sheet content on the mechanical properties of aggregates during amyloid fibrillization
Giovanni Dietler, Hilal Lashuel, Francesco Simone Ruggeri, Jae Sun Jeong, Raffaele Mezzenga
Amyloid fibrils associated with neurodegenerative diseases, such as Parkinson's and Alzheimer's, consist of insoluble aggregates of α-synuclein and Aβ-42 proteins with a high β-sheet content. The aggregation of both proteins occurs by misfolding of the mon ...
Wiley-Blackwell2015Real-time Protein Aggregation Monitoring with a Bloch Surface Wavebased Approach
Hans Peter Herzig, Elsie Barakat, Sara Santi
The misfolding and aggregation of amyloid proteins has been associated with incurable diseases such as Alzheimer's or Parkinson's disease. In the specific case of Alzheimer's disease, recent studies have shown that cell toxicity is caused by soluble oligom ...
Spie-Int Soc Optical Engineering2014