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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 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...
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Protein Folding

Overview
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-protein Interfaces02:04

Protein-protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a polypeptide...
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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Updated: Jun 14, 2026

Preparation of Mechanically Stable Self-Assembled Peptides Hydrogels
05:24

Preparation of Mechanically Stable Self-Assembled Peptides Hydrogels

Published on: September 6, 2024

Interaction between a self-assembling peptide and hydrophobic compounds.

Fushan Tang1, Xiaojun Zhao

  • 1West China Hospital Institute for Nanobiomedical Technology and Membrane Biology, West China Hospital, Sichuan University, No. 1 Ke Yuan 4th Street, Gao Peng Road, Chengdu 610041, Sichuan, China.

Journal of Biomaterials Science. Polymer Edition
|March 27, 2010
PubMed
Summary
This summary is machine-generated.

Self-assembling peptide RAD16-I effectively encapsulates hydrophobic compounds like pyrene, driven by hydrophobic interactions. This demonstrates RAD16-I

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Solubility of Hydrophobic Compounds in Aqueous Solution Using Combinations of Self-assembling Peptide and Amino Acid

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Preparation of Mechanically Stable Self-Assembled Peptides Hydrogels
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Solubility of Hydrophobic Compounds in Aqueous Solution Using Combinations of Self-assembling Peptide and Amino Acid
05:08

Solubility of Hydrophobic Compounds in Aqueous Solution Using Combinations of Self-assembling Peptide and Amino Acid

Published on: September 20, 2017

Area of Science:

  • Biomaterials Science
  • Nanotechnology
  • Supramolecular Chemistry

Background:

  • Hydrophobic compounds often exhibit poor solubility in aqueous environments.
  • Self-assembling peptides offer potential for novel drug delivery systems.
  • Understanding peptide-hydrophobic compound interactions is crucial for developing effective carriers.

Purpose of the Study:

  • To investigate the hydrophobic interaction between self-assembling peptide RAD16-I and a model hydrophobic compound, pyrene.
  • To explore the potential of RAD16-I as a carrier for hydrophobic substances.
  • To elucidate the encapsulation mechanism using biophysical techniques.

Main Methods:

  • Formation of colloidal suspensions of pyrene and RAD16-I.
  • Fluorescence spectroscopy to analyze pyrene's microenvironment.
  • Atomic Force Microscopy (AFM) to visualize aggregate structures.
  • Assay of pyrene transfer into egg phosphatidylcholine vesicles.

Main Results:

  • Increased RAD16-I concentration enhanced pyrene fluorescence intensity.
  • Changes in pyrene emission spectra (I(1)/I(3) and I(1)/I(5) ratios) indicated a non-polar environment.
  • AFM images revealed differences in RAD16-I aggregates with and without pyrene.
  • Pyrene successfully transferred from RAD16-I suspensions to lipid vesicles, confirming carrier potential.

Conclusions:

  • RAD16-I self-assembles and interacts favorably with hydrophobic compounds via hydrophobic interactions.
  • Pyrene preferentially partitions into the non-polar regions of RAD16-I aggregates.
  • RAD16-I shows promise as a carrier for hydrophobic drugs and other molecules.