Related Experiment Video
Updated: Jun 25, 2025

08:53
Characterization of pH-Dependent Reversible Self-Assembly of Amyloid Beta 1-40-Coated Gold Colloids
Published on: March 21, 2025
662
Factors influencing amyloid fibril formation
Fereshteh Ramezani Khorsand1, Fatemeh Aziziyan1, Khosro Khajeh1
1Department of Biochemistry, Faculty of Biological Sciences, Tarbiat Modares University, Tehran, Iran.
Summary
Protein aggregation, a complex process, is influenced by internal and external factors. Understanding these causes is crucial for controlling protein aggregation in research and biopharmaceutical development.
Area of Science:
- Biochemistry
- Molecular Biology
- Protein Science
Background:
- Protein aggregation is a multi-stage process.
- Aggregates exhibit variable stability and toxicity.
- Aggregation impacts protein function and can lead to undesirable properties like immunogenicity.
Purpose of the Study:
- To review intrinsic pathways of protein aggregation.
- To explore extrinsic variables influencing protein aggregation.
- To highlight the importance of understanding and controlling protein aggregation.
Main Methods:
- Review of intrinsic protein aggregation pathways.
- Analysis of extrinsic factors affecting protein aggregation.
- Literature synthesis on protein aggregation mechanisms.
Main Results:
- Identified numerous internal factors (mutations, expression levels, truncation).
- Cataloged external factors (molecular crowding, PTMs, interactions).
- Detailed the impact of aggregation on biological activity and aggregate properties.
Conclusions:
- Protein aggregation is a complex phenomenon driven by diverse factors.
- Controlling protein aggregation is vital for academic and biopharmaceutical research.
- Further research into aggregation pathways and control mechanisms is warranted.
Related Concept Videos
Amyloid Fibrils
9.5K
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 deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining,...
9.5K
Protein Folding
117.8K
Overview
117.8K

