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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...

Conservation of Protein Domains Over Different Proteins

Conservation of Protein Domains Over Different Proteins

Protein domains are small structurally independent units that are part of a single amino acid chain. Although these domains are often structurally independent, they may rely on synergistic effects to perform their functions as part of a larger protein. Protein domains may be conserved within the same organism, as well as across different organisms.
A limited set of protein domains often duplicate and recombine during evolution. These domains can be organized in different combinations to form...

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Related Experiment Video

Updated: May 26, 2026

Rapid Generation of Amyloid from Native Proteins In vitro

Rapid Generation of Amyloid from Native Proteins In vitro

Published on: December 5, 2013

Reverse-engineering amyloid strains with generative protein design.

Laxmikant Gadhe^1,2,3, Katerina Konstantoulea^1,2,3, Aneesh Mazumder^1,2,3

¹Center for Alzheimer's and Neurodegenerative Diseases, University of Texas Southwestern Medical Center, Dallas, TX, USA.

Biorxiv : the Preprint Server for Biology

|May 25, 2026

Summary

This summary is machine-generated.

Generative protein design reveals that diverse amino acid sequences can encode common amyloid fibril architectures. This work explores sequence-structure relationships in amyloid strains and enables engineering of novel fibrillar assemblies.

More Related Videos

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

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

Published on: April 28, 2022

Related Experiment Videos

Last Updated: May 26, 2026

Rapid Generation of Amyloid from Native Proteins In vitro

Rapid Generation of Amyloid from Native Proteins In vitro

Published on: December 5, 2013

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

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

Published on: April 28, 2022

Area of Science:

Biochemistry
Structural Biology
Computational Biology

Background:

Amyloid fibrils exhibit polymorphism, forming distinct structural strains with varied biological impacts.
The relationship between protein sequence and amyloid fibril structure, particularly strain diversity, is not well understood.

Purpose of the Study:

To investigate how amino acid sequences dictate amyloid fibril architectures using generative protein design.
To explore the sequence-structure compatibility landscape for amyloid strains, using alpha-synuclein as a model.

Main Methods:

Applied generative protein design to sample sequence space under structural constraints for defined fibril architectures.
Designed novel sequences and experimentally validated their assembly into fibrils and strain-like behaviors.
Utilized energetic analysis to understand compensatory interactions governing stability.

Main Results:

Identified a continuous compatibility manifold where diverse sequences encode common amyloid architectures.
Engineered de novo sequences that assemble into fibrils with enhanced aggregation efficiency compared to alpha-synuclein.
Demonstrated strain-like properties in designed sequences, including cross-templating and induction of cellular propagation.

Conclusions:

Established a framework for understanding amyloid polymorphism and sequence-structure relationships through generative design.
Showcased generative protein design as a powerful strategy to explore and engineer amyloid fibril structures.
Highlighted the potential for engineering fibrillar protein assemblies and functional biomaterials.