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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,...

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Related Experiment Video

Updated: Sep 26, 2025

Use of Two Dimensional Semi-denaturing Detergent Agarose Gel Electrophoresis to Confirm Size Heterogeneity of Amyloid or Amyloid-like Fibers

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Published on: April 26, 2018

Dendrimers as Antiamyloid Agents.

Svetlana A Sorokina¹, Zinaida B Shifrina¹

¹A.N. Nesmeyanov Institute of Organoelement Compounds, Russian Academy of Sciences, 28 Vavilov St., 119991 Moscow, Russia.

|April 23, 2022

Summary

Dendrimer-protein interactions alter protein structure and behavior, enabling applications in nanomedicine and treating neurodegenerative diseases by preventing protein aggregation.

Keywords:

amyloid diseases antiamyloid activity dendrimers molecular dynamic proteins

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Area of Science:

Biochemistry
Materials Science
Nanotechnology

Background:

Dendrimer-protein conjugates show promise for biological applications.
Complexation significantly alters the biophysical properties of both proteins and dendrimers.
These modifications open avenues for nanotheranostics and biomedicine.

Purpose of the Study:

To review the mechanism and driving forces behind protein-dendrimer interactions.
To explore the therapeutic potential arising from these interactions.
To outline the antiamyloid activity of dendrimers and influencing factors.

Main Methods:

Literature review focusing on protein-dendrimer complexation.
Analysis of how dendrimers affect protein secondary structure, charge, and interactions.
Examination of factors influencing dendrimer antiamyloid properties.

Main Results:

Dendrimer complexation influences protein secondary structure, zeta-potential, and charged region distribution.
Stable complexes can prevent protein aggregation, crucial for neurodegenerative disease therapy.
Dendrimers exhibit antiamyloid activity, modulated by their structure and environmental factors.

Conclusions:

Understanding protein-dendrimer interactions is key to harnessing their therapeutic potential.
Dendrimer-protein conjugates offer a promising platform for nanomedicine and disease treatment.
Further research into dendrimer structure-activity relationships can optimize antiamyloid therapies.