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Related Concept Videos

Protein Folding01:22

Protein Folding

Overview
Protein and Protein Structure02:15

Protein 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...
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...
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...
Protein Folding01:25

Protein 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...
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...

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Related Experiment Video

Updated: Jun 28, 2026

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides
07:26

Formation of Ordered Biomolecular Structures by the Self-assembly of Short Peptides

Published on: November 21, 2013

Water-soluble beta-sheet models which self-assemble into fibrillar structures

K Janek1, J Behlke, J Zipper

  • 1Institute of Molecular Pharmacology, Max Delbrück Center of Molecular Medicine, Institute of Crystallography, Free University, Berlin, Germany.

Biochemistry
|July 1, 1999
PubMed
Summary

Researchers developed water-soluble de novo beta-sheet peptides that self-assemble into fibrillar structures, mimicking amyloid formation. These novel peptides facilitate the study of protein aggregation and beta-sheet stability in neurodegenerative diseases.

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09:54

Synthesis and Characterization of 1,2-Dithiolane Modified Self-Assembling Peptides

Published on: August 20, 2018

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Biophysics

Background:

  • Protein misfolding and aggregation into beta-sheet structures, forming amyloids, are implicated in neurodegenerative diseases like Alzheimer's.
  • Studying these pathogenic protein aggregates is challenging due to their poor solubility.

Purpose of the Study:

  • To design and characterize novel, water-soluble de novo beta-sheet peptides that self-assemble into fibrillar structures.
  • To investigate the relationship between beta-sheet stability and the association behavior of these model peptides.

Main Methods:

  • Synthesis of de novo peptides with varying lengths and D-amino acid substitutions.
  • Conformational analysis using circular dichroism (CD) and Fourier transform infrared spectroscopy (FTIR).
  • Investigation of association behavior via analytical ultracentrifugation and dynamic light scattering (DLS).
  • Characterization of fibril morphology using Congo Red staining and electron microscopy.

Main Results:

  • Peptide length, D-amino acid substitution, and concentration influence beta-sheet formation and stability.
  • Water-soluble beta-sheet complexes with high molecular masses (>2000 kDa) were formed by peptides with n >= 6.
  • These complexes self-assembled into fibrillar structures exhibiting similarities to natural amyloid fibrils.

Conclusions:

  • The developed de novo peptides provide a valuable model system for studying the fundamental principles of beta-sheet self-assembly and amyloid formation.
  • These water-soluble peptide models overcome solubility limitations, enabling detailed investigation of aggregation mechanisms relevant to neurodegenerative diseases.