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Related Concept Videos

Amyloid Fibrils03:03

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, normally used to...
Amyloid Fibrils03:03

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, normally used to...
Fibrous Proteins00:55

Fibrous Proteins

Fibrous proteins are either long and narrow proteins or assemble to form long and thin structures. They contain repetitive units and usually consist of either alpha helices or beta sheets and, in rare cases, a mix of both. The amino acids in the primary structure often consist of repeating amino acid sequences. The role of fibrous proteins is primarily structural. Many are located in the extracellular matrix and are present in connective tissues to impart strength and joint mobility. They are...
Globular and Fibrous Proteins02:21

Globular and Fibrous Proteins

Many proteins can be classified into two distinct subtypes - globular or fibrous. These two types differ in their shapes and solubilities.
Globular proteins are also known as spheroproteins and typically are approximately round in shape. They contain a mix of amino acid types and contain differing sequences in their primary structures. Globular proteins have many different functions, such as enzymes, cellular messengers, and molecular transporters. These roles often require the proteins to be...
Globular and Fibrous Proteins02:21

Globular and Fibrous Proteins

Many proteins can be classified into two distinct subtypes - globular or fibrous. These two types differ in their shapes and solubilities.
Globular proteins are also known as spheroproteins and typically are approximately round in shape. They contain a mix of amino acid types and contain differing sequences in their primary structures. Globular proteins have many different functions, such as enzymes, cellular messengers, and molecular transporters. These roles often require the proteins to be...
Protein Folding01:22

Protein Folding

Overview

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Related Experiment Video

Updated: Jun 21, 2026

Characterizing Individual Protein Aggregates by Infrared Nanospectroscopy and Atomic Force Microscopy
12:58

Characterizing Individual Protein Aggregates by Infrared Nanospectroscopy and Atomic Force Microscopy

Published on: September 12, 2019

Protein aggregation: more than just fibrils.

Mark R H Krebs1, Kristin R Domike, Athene M Donald

  • 1Cavendish Laboratory, University of Cambridge, JJ Thomson Avenue, Cambridge CB3 0HE, UK.

Biochemical Society Transactions
|July 21, 2009
PubMed
Summary
This summary is machine-generated.

Misfolded proteins can form amorphous nanoparticles near their isoelectric point or organized spherulites away from it. These protein aggregates have implications for disease and potential applications like drug delivery.

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Last Updated: Jun 21, 2026

Characterizing Individual Protein Aggregates by Infrared Nanospectroscopy and Atomic Force Microscopy
12:58

Characterizing Individual Protein Aggregates by Infrared Nanospectroscopy and Atomic Force Microscopy

Published on: September 12, 2019

Evaluation of the Impact of Protein Aggregation on Cellular Oxidative Stress in Yeast
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Biochemical Purification and Proteomic Characterization of Amyloid Fibril Cores from the Brain
09:00

Biochemical Purification and Proteomic Characterization of Amyloid Fibril Cores from the Brain

Published on: April 28, 2022

Area of Science:

  • Biochemistry
  • Materials Science
  • Pathology

Background:

  • Protein misfolding and aggregation into amyloid fibrils are implicated in various diseases.
  • Alternative aggregation pathways beyond amyloid fibrils are increasingly recognized.

Purpose of the Study:

  • To investigate the diverse structural outcomes of protein aggregation.
  • To characterize non-fibrillar protein aggregates and their formation conditions.

Main Methods:

  • Exploration of protein aggregation under varying conditions, including isoelectric point and pH.
  • Characterization of aggregate structures using techniques like polarizing light microscopy.

Main Results:

  • Near the isoelectric point, proteins form quasi-amorphous nanoparticles with limited beta-sheet structure.
  • Away from the isoelectric point, proteins form spherulites, which are suprafibrillar aggregates of radiating fibrils.
  • Spherulites exhibit a characteristic Maltese cross shape under polarized light microscopy.

Conclusions:

  • Protein aggregation can yield distinct structures, including amorphous nanoparticles and organized spherulites.
  • These structures form under specific conditions related to charge and pH.
  • Nanoparticles show potential for applications such as controlled drug release.
  • Spherulites, observed both in vitro and in vivo, represent a generic aggregation pathway whose equilibrium with free fibrils requires further study.