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Related Concept Videos

Amyloid Fibrils03:03

Amyloid Fibrils

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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,...
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Amyloid Fibrils03:03

Amyloid Fibrils

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Fibril-associated Collagen01:11

Fibril-associated Collagen

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Fibril-associated collagens are a type of collagens present in the extracellular matrix with interrupted triple helices or FACIT (Fibril-associated collagens interrupted triple-helices). FACIT help connect and attach the collagen fibrils with each other as well as with other proteins of the extracellular matrix.
For example, the type II collagen fibrils in cartilage have covalently bound type IX fibril-associated collagens at regular intervals. Other types of fibril-associated collagens are...
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Turnover Number and Catalytic Efficiency01:19

Turnover Number and Catalytic Efficiency

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The turnover number of an enzyme is the maximum number of substrate molecules it can transform per unit time. Turnover numbers for most enzymes range from 1 to 1000 molecules per second. Catalase has the known highest turnover number, capable of converting up to 2.8×106 molecules of hydrogen peroxide into water and oxygen per second. Lysozyme has the lowest known turnover number of half a molecule per second.
Chymotrypsin is a pancreatic enzyme that breaks down proteins during digestion....
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Catalytically Perfect Enzymes01:07

Catalytically Perfect Enzymes

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The theory of catalytically perfect enzymes was first proposed by W.J. Albery and J. R. Knowles in 1976. These enzymes catalyze biochemical reactions at high-speed. Their catalytic efficiency values range from 108-109 M-1s-1. These enzymes are also called 'diffusion-controlled' as the only rate-limiting step in the catalysis is that of the substrate diffusion into the active site. Examples include triose phosphate isomerase, fumarase, and superoxide dismutase.
 
Most enzymes...
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Reduction of Alkenes: Catalytic Hydrogenation02:13

Reduction of Alkenes: Catalytic Hydrogenation

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Alkenes undergo reduction by the addition of molecular hydrogen to give alkanes. Because the process generally occurs in the presence of a transition-metal catalyst, the reaction is called catalytic hydrogenation.
Metals like palladium, platinum, and nickel are commonly used in their solid forms — fine powder on an inert surface. As these catalysts remain insoluble in the reaction mixture, they are referred to as heterogeneous catalysts.
The hydrogenation process takes place on the...
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Related Experiment Video

Updated: Jan 30, 2026

Interactions with and Membrane Permeabilization of Brain Mitochondria by Amyloid Fibrils
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Interactions with and Membrane Permeabilization of Brain Mitochondria by Amyloid Fibrils

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Catalytic Amyloids: Turning Fibrils Into Biocatalysts.

Alessandra Esposito1, Linda Leone1, Flavia Nastri1

  • 1Department of Chemical Sciences, University of Napoli Federico II, Napoli, Italy.

Chemistry (Weinheim an Der Bergstrasse, Germany)
|January 29, 2026
PubMed
Summary

Catalytic amyloids merge enzyme efficiency with robust nanomaterial properties. This review explores their development and application as stable scaffolds for catalysis and enzyme immobilization, creating innovative biomaterials.

Keywords:
amyloidsbiocatalysismetalloenzymesnanomaterialspeptides

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Biochemical Purification and Proteomic Characterization of Amyloid Fibril Cores from the Brain
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Biochemical Purification and Proteomic Characterization of Amyloid Fibril Cores from the Brain

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Purification and Refolding to Amyloid Fibrils of His6-tagged Recombinant Shadoo Protein Expressed as Inclusion Bodies in E. coli
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Purification and Refolding to Amyloid Fibrils of His6-tagged Recombinant Shadoo Protein Expressed as Inclusion Bodies in E. coli

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Biochemical Purification and Proteomic Characterization of Amyloid Fibril Cores from the Brain
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Purification and Refolding to Amyloid Fibrils of His6-tagged Recombinant Shadoo Protein Expressed as Inclusion Bodies in E. coli
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Area of Science:

  • Biomaterials Science
  • Nanotechnology
  • Catalysis

Background:

  • Amyloids were historically linked to neurodegenerative diseases.
  • Recent discoveries highlight their physiological roles and self-assembly into stable scaffolds.
  • This opens avenues for novel applications in materials science and nanotechnology.

Purpose of the Study:

  • To review the structural and functional properties of natural amyloids and their nanotechnology applications.
  • To survey the development of catalytic amyloids, including bioinspired and de novo designs.
  • To illustrate the use of amyloid fibrils for enzyme immobilization.

Main Methods:

  • Overview of natural amyloid properties and applications.
  • Survey of catalytic amyloid development strategies.
  • Examples of amyloid fibrils as platforms for enzyme immobilization.

Main Results:

  • Amyloids possess unique self-assembly properties suitable for nanomaterial development.
  • Incorporation of functional groups imparts catalytic activity to amyloid fibrils.
  • Amyloid fibrils serve as effective platforms for enzyme immobilization, enhancing catalytic efficiency.

Conclusions:

  • Catalytic amyloids represent a new class of nanomaterials combining enzymatic efficiency with heterogeneous catalyst robustness.
  • Bridging amyloid structures and catalytic activities enables the creation of innovative nanomaterials for diverse applications.
  • Amyloid-based nanomaterials offer a promising platform for advanced catalysis and biocatalysis.