Journal ArticleDOI
Engineering amyloidogenicity towards the development of nanofibrillar materials.
TLDR
The use of amyloid fibrils as structural templates for constructing nanowires has been demonstrated and could potentially become one of the next trends in protein engineering and nanobiotechnology.About:
This article is published in Trends in Biotechnology.The article was published on 2004-02-01. It has received 99 citations till now. The article focuses on the topics: Nanobiotechnology.read more
Citations
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Journal ArticleDOI
Functional π-Gelators and Their Applications
Journal ArticleDOI
Templated Techniques for the Synthesis and Assembly of Plasmonic Nanostructures
Journal ArticleDOI
Controlled patterning of aligned self-assembled peptide nanotubes
TL;DR: The formation of a vertically aligned nanoforest by axial unidirectional growth of a dense array of peptide tubes is shown, demonstrating the ability to form a two-dimensional dense arrays of nanotube assemblies with either vertical or horizontal patterns.
Journal ArticleDOI
Molecular recycling within amyloid fibrils.
Natàlia Carulla,Gemma L. Caddy,Damien Hall,Jesús Zurdo,Margarida Gairí,Miguel Feliz,Ernest Giralt,Carol V. Robinson,Christopher M. Dobson +8 more
TL;DR: Investigation of the nature of the amyloid structure by monitoring hydrogen/deuterium exchange in fibrils formed from an SH3 domain using a combination of nuclear magnetic resonance spectroscopy and electrospray ionization mass spectrometry reveals that exchange is dominated by a mechanism of dissociation and re-association that results in the recycling of molecules within the fibril population.
Journal ArticleDOI
Biotemplated Nanostructured Materials
TL;DR: The potential of biological scaffolds for the fabrication of novel types of nanostructures is explored in this article, where the authors present an overview of the biological template-based approach for the synthesis and organization of inorganic nanostructure into well-defined architectures.
References
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PatentDOI
Self-assembly and mineralization of peptide-amphiphile nanofibers
TL;DR: In this paper, pH-induced self-assembly of a peptide-amphiphile was used to make a nanostructured fibrous scaffold reminiscent of extracellular matrix.
Journal ArticleDOI
Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases.
Monica Bucciantini,Elisa Giannoni,Fabrizio Chiti,Fabrizio Chiti,Fabiana Baroni,Lucia Formigli,Jesús Zurdo,Niccolò Taddei,Giampietro Ramponi,Christopher M. Dobson,Massimo Stefani +10 more
TL;DR: This finding provides added evidence that avoidance of protein aggregation is crucial for the preservation of biological function and suggests common features in the origins of this family of protein deposition diseases.
Journal ArticleDOI
Casting Metal Nanowires Within Discrete Self-Assembled Peptide Nanotubes
Meital Reches,Ehud Gazit +1 more
TL;DR: The observation of the self-assembly of a very short peptide, the Alzheimer's β-amyloid diphenylalanine structural motif, into discrete and stiff nanotubes, resulted in the production of discrete nanowires with a long persistence length.
Journal ArticleDOI
Quality control in the endoplasmic reticulum
Lars Ellgaard,Ari Helenius +1 more
TL;DR: Recent progress is discussed in understanding the conformation-specific sorting of proteins at the level of ER retention and export, which is important for the fidelity of cellular functions.
Journal ArticleDOI
A structural model for Alzheimer's β-amyloid fibrils based on experimental constraints from solid state NMR
Aneta T. Petkova,Yoshitaka Ishii,John J. Balbach,Oleg N. Antzutkin,Richard D. Leapman,Frank Delaglio,Robert Tycko +6 more
TL;DR: A structural model for amyloid fibrils formed by the 40-residue β-amyloid peptide associated with Alzheimer's disease (Aβ1–40) is presented, based on a set of experimental constraints from solid state NMR spectroscopy and incorporates the cross-β structural motif established by x-ray fiber diffraction.
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Casting Metal Nanowires Within Discrete Self-Assembled Peptide Nanotubes
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