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Peptide Bonds02:43

Peptide Bonds

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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...
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Dehydration Synthesis01:15

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Overview
Dehydration synthesis (also called a condensation reaction) is the chemical process in which two molecules covalently link together to form a new molecule, along with the release of a water molecule. Many physiologically important compounds form by dehydration synthesis reactions, such as complex carbohydrates, proteins, DNA, and RNA.
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Transfer RNA Synthesis02:36

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One of the unique features of tRNA is the presence of modified bases. In some tRNAs, modified bases account for nearly 20% of the total bases in the molecule. Altogether, these unusual bases protect the tRNA from enzymatic degradation by RNases.
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Ribosome synthesis is a highly complex and coordinated process involving more than 200 assembly factors. The synthesis and processing of ribosomal components occurs not only in the nucleolus but also in the nucleoplasm and the cytoplasm of eukaryotic cells.
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Protein Complex Assembly02:41

Protein Complex Assembly

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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.
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Synthesis and Decomposition Reactions02:17

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Synthesis and decomposition are two types of redox reactions. Synthesis means to make something, whereas decomposition means to break something. The reactions are accompanied by chemical and energy changes. 
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Updated: Feb 5, 2026

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

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

Ruben Neves1, Kailyn Stephens1, Jillian E Smith-Carpenter2

  • 1Department of Chemistry and Biochemistry, Fairfield University.

Journal of Visualized Experiments : Jove
|September 4, 2018
PubMed
Summary

Researchers synthesized a 1,2-dithiolane modified peptide, derived from Alzheimer's disease-associated Aβ peptide, which self-assembles into cross-β amyloid fibers. This work enables new strategies for modifying peptide assemblies using dynamic covalent chemistry.

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Split-and-pool Synthesis and Characterization of Peptide Tertiary Amide Library

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Area of Science:

  • Supramolecular Chemistry
  • Biomaterials Science
  • Neuroscience

Background:

  • Self-assembling peptides are crucial for developing novel biomaterials.
  • Amyloid fibers, like those from the Aβ peptide, are implicated in Alzheimer's disease.
  • Controlling the assembly and modification of peptides is key for therapeutic and diagnostic applications.

Purpose of the Study:

  • To synthesize a 1,2-dithiolane modified self-assembling peptide.
  • To characterize the self-assembled supramolecular structures formed by this modified peptide.
  • To establish a platform for exploring post-assembly modification strategies and dynamic covalent chemistry on peptide nanofibers.

Main Methods:

  • Solid-phase peptide synthesis with on-resin coupling of a dithiolane precursor.
  • Microwave-assisted thioacetate deprotection and final cleavage from the resin.
  • High-performance liquid chromatography (HPLC) for purification.
  • Characterization using Fourier-transform infrared spectroscopy (FT-IR), circular dichroism spectroscopy (CD), and transmission electron microscopy (TEM).

Main Results:

  • Successful synthesis of an N-terminus 1,2-dithiolane modified peptide.
  • Demonstration that the modified peptide self-assembles into cross-β amyloid fibers.
  • Detailed characterization of the resulting amyloid fiber morphology and structure.

Conclusions:

  • N-terminal modification with a 1,2-dithiolane moiety is feasible for self-assembling peptides.
  • The modified peptide serves as a model system for creating functionalized amyloid fibers.
  • This approach opens avenues for dynamic covalent chemistry on peptide nanofiber surfaces for advanced biomaterial applications.