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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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Related Experiment Video

Updated: Jun 14, 2025

Synthesis and Characterization of 1,2-Dithiolane Modified Self-Assembling Peptides

Synthesis and Characterization of 1,2-Dithiolane Modified Self-Assembling Peptides

Published on: August 20, 2018

Amino Acid-Based Self-Assembled Supramolecular Structures: From Pathological Implications to Biomedical Applications.

Pooja Sharma¹, Prabhjot Singh², Neelam^1,3

¹Department of Applied Sciences, University Institute of Engineering and Technology (U.I.E.T), Panjab University, Sector 25, Chandigarh, 160025, India.

Chembiochem : a European Journal of Chemical Biology

|May 14, 2025

Summary

Amino acids and peptides can spontaneously self-assemble into supramolecular structures. This review explores their pathological and functional roles, highlighting applications in material science and biomedicine.

Keywords:

amino acids biomedical applications drug deliveries nanostructures neurotoxicities self‐assemblies

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Facile Protocol for the Synthesis of Self-assembling Polyamine-based Peptide Amphiphiles PPAs and Related Biomaterials

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Last Updated: Jun 14, 2025

Synthesis and Characterization of 1,2-Dithiolane Modified Self-Assembling Peptides

Synthesis and Characterization of 1,2-Dithiolane Modified Self-Assembling Peptides

Published on: August 20, 2018

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides

Published on: November 21, 2013

Facile Protocol for the Synthesis of Self-assembling Polyamine-based Peptide Amphiphiles PPAs and Related Biomaterials

Facile Protocol for the Synthesis of Self-assembling Polyamine-based Peptide Amphiphiles PPAs and Related Biomaterials

Published on: June 25, 2018

Area of Science:

Biomolecular chemistry
Nanotechnology
Material Science

Background:

Self-assembly is the spontaneous organization of molecules into supramolecular structures, mimicking natural biomolecules like DNA and proteins.
The "FF" moiety's role in protein self-aggregation, particularly in amyloids, is crucial for peptide nanotechnology.
Amino acids, as peptide building blocks, are fundamental to understanding and designing self-assembled nanomaterials.

Purpose of the Study:

To systematically review recent findings on amino acid-based self-assembly.
To discuss the pathological and functional roles of self-assembled amino acids and peptides.
To highlight emerging applications of self-assembled amino acid-based nanomaterials in material science and biomedicine.

Main Methods:

Literature review of recent findings on amino acid self-assembly.
Systematic overview of self-assembly mechanisms and properties.
Analysis of pathological and functional implications.

Main Results:

Amino acid and peptide self-assembly leads to diverse supramolecular structures.
Self-assembly has significant implications in biomedical fields like drug delivery, biosensing, and tissue engineering.
The "FF" moiety is a key factor in self-aggregation, driving advancements in peptide nanotechnology.

Conclusions:

Understanding amino acid self-assembly is vital for designing advanced functional materials.
Self-assembled amino acid-based nanomaterials offer promising futuristic applications in material science and biomedicine.
This review provides a comprehensive overview of the field, emphasizing its potential impact.