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Related Concept Videos

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.
Protein Structure Is Critical to Its Biological Function
Proteins perform a wide range of biological functions such as catalyzing chemical reactions, providing...
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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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Protein and Protein Structure02:15

Protein and Protein Structure

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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.
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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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Molecular Chaperones and Protein Folding03:00

Molecular Chaperones and Protein Folding

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The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
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Related Experiment Video

Updated: Mar 29, 2026

Synthesis and Characterization of 1,2-Dithiolane Modified Self-Assembling Peptides
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Electrostatic-Driven Lamination and Untwisting of β-Sheet Assemblies.

Yang Hu1, Ran Lin, Pengcheng Zhang

  • 1Department of Chemical Engineering, Tsinghua University , Beijing 100084, China.

ACS Nano
|December 10, 2015
PubMed
Summary
This summary is machine-generated.

Electrostatic interactions control peptide assembly. Repulsions lead to twisted fibrils, while reduced repulsion forms belt-like structures, aiding biomaterial design.

Keywords:
electrostatic interactionnanostructurespeptidesself-assemblyβ-sheet tapes

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Area of Science:

  • Biomaterials Science
  • Supramolecular Chemistry
  • Nanotechnology

Background:

  • One-dimensional (1D) peptide nanostructures are crucial in disease and biomaterials.
  • Filamentous assemblies often use beta-sheet sequences but exhibit diverse morphologies.
  • Understanding beta-sheet stacking is key to controlling peptide assembly polymorphism.

Purpose of the Study:

  • To investigate the role of electrostatic interactions in the lamination and untwisting of 1D peptide assemblies.
  • To elucidate how molecular design influences beta-sheet stacking and nanostructure morphology.
  • To provide insights for the rational design of functional peptide-based materials.

Main Methods:

  • Design and synthesis of three short peptides (EFFFFE, KFFFFK, EFFFFK) with varying terminal charges.
  • Characterization of the self-assembly behavior and resulting nanostructure morphologies.
  • Analysis of the influence of electrostatic interactions on beta-sheet stacking and assembly twisting.

Main Results:

  • Electrostatic repulsions between terminal charges decrease the pitch of twisting beta-sheet tapes.
  • This repulsion leads to the formation of highly twisted, intertwined fibrils or twisted ribbons.
  • Reduced electrostatic repulsion, via opposite terminal charges or coassembly, promotes infinite, belt-like assemblies.

Conclusions:

  • Electrostatic interactions are decisive in controlling the lamination and untwisting of 1D peptide assemblies.
  • Molecular design of terminal charges offers effective control over beta-sheet stacking and nanostructure morphology.
  • These findings provide a fundamental understanding for designing tailored beta-sheet assemblies and functional peptide biomaterials.