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Amyloid Fibrils

Amyloid Fibrils

Amyloid fibrils are aggregates of misfolded proteins. Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils.
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining, normally used to...

Amyloid Fibrils

Amyloid Fibrils

Amyloid fibrils are aggregates of misfolded proteins. Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils.
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining, normally used to...

Protein-protein Interfaces

Protein-protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a polypeptide...

Ionic Crystal Structures

Ionic Crystal Structures

Ionic crystals consist of two or more different kinds of ions that usually have different sizes. The packing of these ions into a crystal structure is more complex than the packing of metal atoms that are the same size.
Most monatomic ions behave as charged spheres, and their attraction for ions of opposite charge is the same in every direction. Consequently, stable structures for ionic compounds result (1) when ions of one charge are surrounded by as many ions as possible of the opposite...

Polymer Classification: Crystallinity

Polymer Classification: Crystallinity

Unlike ionic or small covalent molecules, polymers do not form crystalline solids due to the diffusion limitations of their long-chain structures. However, polymers contain microscopic crystalline domains separated by amorphous domains.
Crystalline domains are the regions where polymer chains are aligned in an orderly manner and held together in proximity by intermolecular forces. For example, chains in the crystalline domains of polyethylene and nylon are bound together by van der Waals...

Imperfections in Crystal Structure: Point, Line and Plane Defects

Imperfections in Crystal Structure: Point, Line and Plane Defects

A perfect crystal, in theory, has a uniform structure with the same unit cell and lattice points throughout. However, any deviation from this periodic arrangement is known as an imperfection or defect. These defects can be categorized into three types: point, line, and plane defects.Point defects occur when there is a deviation from the ideal due to missing atoms, displaced atoms, or additional atoms. These imperfections might occur due to imperfect packing during crystallization or because of...

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Related Experiment Video

Updated: Jun 22, 2026

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy

Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy

Published on: September 17, 2017

Crystalline amyloid structures at interfaces.

Mathilde Lepère¹, Corinne Chevallard, Gerald Brezesinski

¹Laboratoire Interdisciplinaire sur l'Organisation Nanométrique et Supramoléculaire, CEA, IRAMIS, SCM, 91191 Gif-sur-Yvette cedex, France.

Angewandte Chemie (International Ed. in English)

|May 30, 2009

Summary

Amyloid peptides self-assemble into crystalline nanostructures at air-water interfaces. These ordered structures enable controlled inorganic material deposition, mimicking biomineralization processes.

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Atomic Scale Structural Studies of Macromolecular Assemblies by Solid-state Nuclear Magnetic Resonance Spectroscopy

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Area of Science:

Materials Science
Biophysics
Nanotechnology

Background:

Amyloid peptides are known for their self-assembly properties.
Controlling nanostructure formation at interfaces is crucial for advanced materials.
Biomineralization offers a natural model for ordered inorganic material synthesis.

Purpose of the Study:

To investigate the interfacial self-assembly of amyloid peptides into crystalline nanostructures.
To explore the potential of these nanostructures for controlled inorganic material deposition.
To understand the fundamental principles governing self-assembly at air-water interfaces.

Main Methods:

Utilized atomic force microscopy (AFM) to characterize nanostructure morphology.
Employed X-ray diffraction (XRD) to determine the crystalline nature of the self-assembled structures.
Investigated self-assembly at air-water interfaces.

Main Results:

Successfully developed crystalline nanostructures through interfacial self-assembly of amyloid peptides.
Demonstrated the formation of regular arrays of functional groups within the nanostructures.
Observed controlled deposition of inorganic materials on these nanostructures, analogous to biomineralization.

Conclusions:

Interfacial self-assembly of amyloid peptides provides a route to ordered crystalline nanostructures.
These nanostructures serve as templates for controlled inorganic material deposition.
The findings offer insights into biomimetic approaches for materials synthesis.