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Related Concept Videos

Amyloid Fibrils03:03

Amyloid Fibrils

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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. 
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Formation of Higher-order Actin Filaments01:11

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The polymerization of G-actin monomers into filamentous F-actin is a multi-step process. Once the F-actins are formed, they can bundle together in different arrangements to form higher-order networks and regulate cellular functions. Common examples include the formation of lamellipodia and filopodia at the cell's leading edge by actin reorganization in a migrating cell. The microvilli on the brush border epithelial cells are also formed through the F-actin network.
The high-order actin...
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Formation of Intermediate Filaments00:57

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Intermediate filaments are cytoskeletal proteins with higher tensile strength and flexibility than microfilaments and microtubules. Unlike the other two cytoskeletal proteins, intermediate filament formation lacks the enzymatic activity to hydrolyze nucleotides like ATP and GTP to generate energy for polymerization. Therefore, the formation of intermediate filaments is multistep self-assembly. The involvement of any accessory proteins in intermediate filament formation has not yet been...
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Assembly of Cytoskeletal Filaments01:18

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Cytoskeletal filaments are polymeric forms of smaller protein subunits. However, individual cytoskeletal filaments may easily disassemble or associate with other similar filaments to form rigid structures. Microfilaments, made of actin monomers, rely on actin-binding proteins to form bundles and create networks of individual actin filaments. Microtubules rely on microtubule-associated proteins (MAPs) to form sturdy cylindrical structures. However, the proteins involved in forming complex...
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Protein Complex Assembly02:41

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Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
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Protein Folding01:25

Protein Folding

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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.
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Related Experiment Video

Updated: Jun 14, 2025

Characterization of pH-Dependent Reversible Self-Assembly of Amyloid Beta 1-40-Coated Gold Colloids
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Characterization of pH-Dependent Reversible Self-Assembly of Amyloid Beta 1-40-Coated Gold Colloids

Published on: March 21, 2025

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Amylum forms typical self-assembled amyloid fibrils.

Sonika Chibh1, Ashmeet Singh2, Gal Finkelstein-Zuta1,3

  • 1The Shmunis School of Biomedicine and Cancer Research, George S. Wise Faculty of Life Sciences, Tel Aviv University, Tel Aviv 6997801, Israel.

Science Advances
|August 30, 2024
PubMed
Summary
This summary is machine-generated.

Starch (amylum) can self-assemble into amyloid fibrils, exhibiting properties like nanofibril formation and dye binding. This finding expands our understanding of the amyloid phenomenon beyond proteins.

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Rapid Generation of Amyloid from Native Proteins In vitro
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Related Experiment Videos

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Characterization of pH-Dependent Reversible Self-Assembly of Amyloid Beta 1-40-Coated Gold Colloids
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Characterization of pH-Dependent Reversible Self-Assembly of Amyloid Beta 1-40-Coated Gold Colloids

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Rapid Generation of Amyloid from Native Proteins In vitro
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Area of Science:

  • Biochemistry
  • Biophysics
  • Materials Science

Background:

  • Amyloid fibril formation is crucial in both normal physiology and disease pathology.
  • While "amyloid" suggests starch-like properties, polysaccharides have not been shown to form amyloid structures.
  • Research has focused on protein amyloidogenesis and its associated diseases.

Purpose of the Study:

  • To investigate if amylum (starch) can self-assemble into hierarchical fibrillar structures.
  • To determine if starch exhibits canonical amyloidogenic properties.
  • To expand the understanding of the generic amyloid phenomenon.

Main Methods:

  • Inducing ordered amylum structure formation.
  • Characterizing the self-assembly process using sigmoidal growth kinetics.
  • Analyzing fibril morphology, dye binding (e.g., Congo red), luminescence, birefringence, and mechanical properties.

Main Results:

  • Amylum self-assembles into ordered, hierarchical fibrillar structures.
  • These structures display characteristic amyloid features: nanofibril morphology, dye binding, luminescence, and apple-green birefringence.
  • The formation process follows sigmoidal growth kinetics, typical of amyloidogenesis.

Conclusions:

  • Starch (amylum) possesses the ability to form amyloidogenic structures.
  • This study demonstrates canonical amyloid properties in polysaccharides for the first time.
  • Findings broaden the scope of the amyloid phenomenon and polysaccharide self-assembly.