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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,...

Amyloid Fibrils

Amyloid Fibrils

Clot Retraction and Fibrinolysis

Clot Retraction and Fibrinolysis

After a fibrin clot is formed, the next step is clot retraction, a vital process facilitated by platelet contractile proteins, such as actin and myosin. These proteins pull the fibrin strands closer together and condense the clot. This action reduces the size of the clot, creating a smaller, denser structure that effectively seals off the damaged vessel. Clot retraction consolidates the clot and helps with wound healing by bringing the edges of the damaged blood vessel closer together.

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Related Experiment Video

Updated: Dec 26, 2025

Analysis of β-Amyloid-induced Abnormalities on Fibrin Clot Structure by Spectroscopy and Scanning Electron Microscopy

Analysis of β-Amyloid-induced Abnormalities on Fibrin Clot Structure by Spectroscopy and Scanning Electron Microscopy

Published on: November 30, 2018

Modulating Aβ Fibrillogenesis with 'Trojan' peptides.

Gaurav Pandey¹, Sudhir Morla¹, Sachin Kumar¹

¹Department of Biosciences and Bioengineering, Indian Institute of Technology Guwahati, Guwahati, -781039, India.

|March 12, 2020

Summary

This summary is machine-generated.

Researchers designed

Keywords:

Amyloid-beta Peptide-based inhibitors Protein aggregation Trojan peptides

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Analysis of β-Amyloid-induced Abnormalities on Fibrin Clot Structure by Spectroscopy and Scanning Electron Microscopy

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Fabrication of Amyloid-β-Secreting Alginate Microbeads for Use in Modelling Alzheimer's Disease

Published on: July 6, 2019

Area of Science:

Neuroscience and biochemistry, focusing on protein aggregation and neurodegenerative diseases.

Background:

Alzheimer's disease (AD) pathogenesis is linked to abnormal beta-amyloid (Aβ) peptide aggregation into amyloid plaques.
Inhibiting Aβ aggregation presents a promising therapeutic strategy for AD management.

Purpose of the Study:

To design and evaluate 'trojan peptides' for structure-based intervention in Aβ aggregation.
To assess the efficacy of trojan peptides in preventing toxic fibril formation and reducing neuronal cytotoxicity.

Main Methods:

Structure-based design of short peptides targeting the Aβ core recognition domain.
Thioflavin T (ThT) fluorescence assay to monitor aggregation.
Field Emission Transmission Electron Microscopy (FETEM) for imaging.
Infrared (IR) spectroscopy and cytotoxicity assays on neuronal cell lines.

Main Results:

Designed trojan peptides demonstrated the ability to impede Aβ peptide aggregation.
Formation of toxic fibrillar assemblies was arrested by the trojan peptides.
Reduced cytotoxicity was observed in model neuronal cell lines treated with trojan peptides.

Conclusions:

Trojan peptides show potential as a therapeutic approach to inhibit Aβ aggregation in Alzheimer's disease.
These peptides can modulate Aβ self-assembly, reduce fibril formation, and mitigate neuronal cell damage.