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Related Concept Videos

Peptide Bonds02:43

Peptide Bonds

A peptide bond covalently attaches amino acids through a dehydration reaction. One amino acid's carboxyl group and another amino acid's amino group combine, releasing a water molecule. The resulting bond is the peptide bond. The products that such linkages form are peptides. As more amino acids join this growing chain, the resulting chain is a polypeptide. Each polypeptide has a free amino group at one end. This end has the N-terminal, or the amino-terminal, and the other end has a free...
Protein Complex Assembly02:41

Protein Complex Assembly

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.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
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.
Protein Organization01:13

Protein Organization

Overview
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

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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

Self-assembling properties of ionic-complementary peptides.

Gabriella D'Auria1, Manuela Vacatello, Lucia Falcigno

  • 1Department of Chemistry, University of Naples "Federico II", 80126 Naples, Italy. gabriella.dauria@unina.it

Journal of Peptide Science : an Official Publication of the European Peptide Society
|November 22, 2008
PubMed
Summary

Synthetic peptide self-assembly is driven by hydrophobic interactions, with longer peptides showing greater propensity. Aggregation is favored by salt and neutral pH, mimicking beta-amyloid mechanisms.

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Area of Science:

  • Biochemistry
  • Materials Science
  • Biophysics

Background:

  • Self-complementary peptides with alternating polar and nonpolar residues can self-assemble.
  • The EAK16 peptide serves as a prototype for such self-assembling systems.

Purpose of the Study:

  • To investigate the role of charge and hydrophobic interactions in peptide self-assembly.
  • To compare the self-assembling properties of 8-mer and 16-mer peptides.
  • To understand the influence of environmental factors like salt concentration and pH on aggregation.

Main Methods:

  • Circular Dichroism (CD) spectroscopy
  • Nuclear Magnetic Resonance (NMR) spectroscopy
  • Small-angle neutron scattering (SANS)
  • Diffusion measurements

Main Results:

  • 16-mer peptides exhibit higher self-assembly propensity than 8-mer analogs.
  • Aggregation is favored by the presence of salts and neutral pH.
  • Hydrophobic character is the most critical factor influencing self-assembly.
  • Peptides exist as light (monomer/random coil) and heavy (beta-aggregates) forms under mild conditions.
  • In alcohol-water mixtures, peptides can transition from extended conformations to helical structures, with the prototype forming helical monomers and beta-aggregates.

Conclusions:

  • Hydrophobic interactions are paramount for self-assembly of these synthetic peptides.
  • Peptide length significantly impacts self-assembly propensity.
  • Environmental conditions modulate peptide aggregation states.
  • The observed helical to beta-aggregate transition mechanism resembles that of beta-amyloid peptides.