Related Experiment Video
Updated: Jul 20, 2026
05:48
Rapid Generation of Amyloid from Native Proteins In vitro
Published on: December 5, 2013
Sequence and structural determinants of amyloid fibril formation
Francesco Bemporad1, Giulia Calloni, Silvia Campioni
1Dipartimento di Scienze Biochimiche, Università di Firenze, Viale Morgagni 50, 50134 Firenze, Italy.
Accounts of Chemical Research
|September 20, 2006
Summary
Protein aggregation, including amyloid fibril formation, is key in biology and disease. This study explores sequence and structural factors influencing protein aggregation across various states, from unfolded to folded.
Area of Science:
- Biochemistry and Molecular Biology
- Protein Chemistry
- Pathology
Background:
- Protein aggregation is fundamental to protein chemistry and biological processes.
- It plays a critical role in human diseases and the life sciences.
- Understanding aggregation mechanisms is crucial for both basic science and medicine.
Purpose of the Study:
- To review recent findings on sequence and structural determinants of protein aggregation.
- To elucidate factors governing the aggregation of unfolded peptides and proteins.
- To summarize factors influencing the aggregation of partially structured and fully folded proteins.
Main Methods:
- Review of recent scientific literature on protein aggregation.
- Analysis of sequence and structural factors.
- Examination of aggregation pathways for different protein conformational states.
Main Results:
- Identified key sequence and structural determinants influencing protein aggregation.
- Characterized factors that promote aggregation in unfolded peptides and proteins.
- Demonstrated that even fully folded proteins can aggregate into early oligomers without major conformational changes.
Conclusions:
- Protein aggregation is a complex process influenced by sequence and structure.
- Aggregation can occur across multiple protein conformational states, including folded ones.
- Further research into these determinants can advance understanding of protein misfolding diseases.
Related Concept Videos
03:03Amyloid 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 deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining, normally used to...
03:03Amyloid 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 deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining, normally used to...
02:15Protein and Protein Structure
Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
A protein's shape is critical to its function. For example, an enzyme can...
A protein's shape is critical to its function. For example, an enzyme can...
01:22Protein Folding
Overview
01:25Protein Folding
Proteins are chains of amino acids linked together by peptide bonds. Upon synthesis, a protein folds into a three-dimensional conformation, critical to its biological function. Interactions between its constituent amino acids guide protein folding, and hence the protein structure is primarily dependent on its amino acid sequence.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
01:13Protein Organization
Overview