Amyloid fibrils applications

Baldus M (2007) Magnetic resonance in the solid state applications to protein folding, amyloid fibrils and membrane proteins. Eur Biophys J 36(Suppl 1) S37—48... 

Paul van der Schoot, Nucleation and Co-Operativity in Supramolecular Polymers Michael J. McPherson, Kier James, Stuart Kyle, Stephen Parsons, and Jessica Riley, Recombinant Production of Self-Assembling Peptides Boxun Leng, Lei Huang, and Zhengzhong Shao, Inspiration from Natural Silks and Their Proteins Sally L. Gras, Surface- and Solution-Based Assembly of Amyloid Fibrils for Biomedical and Nanotechnology Applications... 

Sally L. Gras, Surface- and Solution-Based Assembly of Amyloid Fibrils for Biomedical and Nanotechnology Applications... 

This chapter describes the self-assembly of non-native protein fibers known as amyloid fibrils and the development of these fibrils for potential applications in nanotechnology and biomedicine. It extends an earlier review by the author on a related topic (Gras, 2007). In Section 1, the self-assembly of polypeptides into amyloid fibrils and efforts to control assembly and any subsequent disassembly are discussed. In Section 2, this review focuses on the important role of surfaces and interfaces during and after polypeptide assembly. It examines how different surfaces can influence fibril assembly, how surfaces can be used to direct self-assembly in order to create highly ordered structures, and how different techniques can be used to create aligned and patterned materials on surfaces following self-assembly. 

In this section, the potential application for amyloid fibrils and other selfassembling fibrous protein structures are outlined. These include potential uses in electronics and photonics presented in Section 4.1, uses as platforms for the immobilization of enzymes and biosensors presented in Section 4.2, and uses as biocompatible materials presented in Section 4.3. Each of these applications makes use of the ability of polypeptides to self-assemble and form nanostructured materials, a process that can occur under aqueous conditions. These applications also seek to exploit the favorable properties of fibrils such as strength and durability, the ability to arrange ligands on a nanoscale, and their potential biocompatibility arising from the natural materials used for assembly. 

The presence of 3-sheet in a protein solution can also be determined using FTIR by inspecting the amide I band, which occurs in the region between 1600 cm and 1700cm and taking into account possible contributions from side chains. Amyloid fibrils typically have 3-sheet peaks below 1620 cm FTIR is not suitable to determine atomic coordinates, but it has given detailed insights into protein structure, and its easy sample preparation and the applicability to most molecules have led to the development of many experimental techniques (reviewed in (56)). 

It is known that many proteins and peptides aggregate into extended p sheet like structures [3], Formation of amyloid fibrils is recognized important not only in understanding of human diseases but also is found acceptable for development of ordered nanostructures with modifiable properties and applicable in biotechnology, material science, molecular electronics and related fields. 

R 96 R. Tycko, Applications of Solid State NMR to the Structural Characterization of Amyloid Fibrils Methods and Results , p. 53... 

R 598 L. K. Thompson, Unraveling the Secrets of Alzheimer s j3-Amyloid Fibrils , P. Natl. Acad. Sci. U. S. A., 2003,100, 383 R 599 T. Timusk, The Mysterious Pseudogap in High Temperature Superconductors An Infrared View , Solid State Commun., 2003,127, 337 R 600 P. A. Tishmack, D. E. Bugay and S. R. Byrn, Solid-State Nuclear Magnetic Resonance Spectroscopy - Pharmaceutical Applications , J. Pharm. Sci., 2003, 92,441... 

The biological and biomedical applications of graphene and its derivatives are currently of great interest and have been reviewed in de-tail. Li and Mezzenga have recently reviewed the interaction of amyloid fibrils with carbon nanomaterials such as graphene, extending the scope of biomedical applications and composite biomaterials, indeed, the supramolecular self-assembly of carbonaceous nanomaterials by biomolecules is now a possibility. ... 

Shi et al. showed examples of the application of 3D solid-state NMR experiments in biology which particularly suitable for the characterisation of insoluble proteins and protein aggregates such as amyloid fibrils, membrane-lipid complexes, and precipitated proteins. ... 

The applicability of high-resolution solid-state NMR spectroscopic techniques to the structure determination of amyloid fibrils of a prion protein has been demonstrated. It has been shown that a satisfactory resolution, up to 0.25 ppm for resonances with resolved /-couplings or 0.5 ppm for those without resolved /-couplings, can be obtained in spectra of amyloid fibrils. 

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