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Related Concept Videos

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...
Protein Folding01:22

Protein Folding

Overview
Protein Organization01:24

Protein Organization

Proteins are polymers of amino acid residues. They are versatile and responsible for different cellular functions, including DNA replication, molecular transport, catalysis, and structural support. Proteins have a hierarchical structure comprising at least three levels of organization: primary, secondary, and tertiary structure. Some large proteins have a quaternary structure where individual protein subunits are linked together.
The primary structure of a protein is its amino acid sequence.

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Synthesis and Structure Determination of µ-Conotoxin PIIIA Isomers with Different Disulfide Connectivities
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Aggregation and conformational studies on a pentapeptide derivative.

Dhandayuthapani Sambasivam1, Corey W Liu, Murali Jayaraman

  • 1Bioorganic and Neurochemistry Laboratory, Central Leather Research Institute, Adyar, Chennai 600 020, India.

Biochimica Et Biophysica Acta
|September 9, 2008
PubMed
Summary

This study explores amyloid fibril formation, suggesting a mix of peptide conformational states is key. Peptide I forms beta-sheet structures but yields unstable fibrils, challenging existing models.

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Last Updated: Jul 1, 2026

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07:26

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

Published on: November 21, 2013

Area of Science:

  • Biochemistry
  • Biophysics
  • Materials Science

Background:

  • Amyloid fibrils, implicated in diseases, are beta-sheet polymers.
  • Not all beta-sheet rich peptides form amyloid fibrils.
  • The role of conformational heterogeneity in fibril stability is unclear.

Purpose of the Study:

  • To test the hypothesis that mixed conformational states are required for stable amyloid-like fibril formation.
  • To investigate the self-assembly and fibril formation of a specific amyloid-forming peptide (HCl(Ile)(5)NH(CH(2)CH(2)O)(3)CH(3), designated as I).

Main Methods:

  • Incubation of peptide I in aqueous buffer.
  • Characterization of self-assembled structures using techniques sensitive to beta-sheet content.
  • Binding assays with amyloidophilic dyes (Congo red, Thioflavin T).

Main Results:

  • Peptide I self-assembles into beta-sheet structures in aqueous solution.
  • These structures exhibit diameters of 30-60 Å and bind to Congo red and Thioflavin T.
  • Prolonged incubation at higher concentrations resulted in unstable fibril formation, contrary to typical amyloid peptide behavior.

Conclusions:

  • The study provides insights into the complex process of amyloid fibril formation.
  • Peptide I's formation of unstable fibrils suggests that conformational heterogeneity may influence fibril stability.
  • Findings challenge the general understanding of mature fibril formation in amyloid peptides.