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Preparation and Reactions of Sulfides

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Sulfides are the sulfur analog of ethers, just as thiols are the sulfur analog of alcohol. Like ethers, sulfides also consist of two hydrocarbon groups bonded to the central sulfur atom. Depending upon the type of groups present, sulfides can be symmetrical or asymmetrical. Symmetrical sulfides can be prepared via an SN2 reaction between 2 equivalents of an alkyl halide and one equivalent of sodium sulfide.
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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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Sulfur Assimilation01:20

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Sulfur is an essential element in biological systems, contributing to synthesizing key biomolecules, including amino acids such as cysteine and methionine, and cofactors such as coenzyme A and biotin. Microorganisms primarily assimilate sulfur as sulfate (SO₄²⁻) from the environment, which must undergo a series of biochemical transformations before it can be incorporated into cellular components. As sulfate is highly oxidized, it must undergo assimilatory sulfate reduction to...
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Chirality is most prevalent in carbon-based tetrahedral compounds, but this important facet of molecular symmetry extends to sp3-hybridized nitrogen, phosphorus and sulfur centers, including trivalent molecules with lone pairs. Here, the lone pair behaves as a functional group in addition to the other three substituents to form an analogous tetrahedral center that can be chiral.
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Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
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Signal sequences are short amino acid sequences that guide newly synthesized proteins to their proper location within the cell. Classical signal sequences are fifteen to sixty amino acids long and present at the N-terminus of a polypeptide chain. Each signal sequence has a conserved segment of basic residues towards their N terminus, a hydrophobic core, and a C-terminus rich in polar residues. The C-terminus also contains a signal cleavage site and features a -3 -1 sequence motif. The -3-1...
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Constructing Thioether/Vinyl Sulfide-tethered Helical Peptides Via Photo-induced Thiol-ene/yne Hydrothiolation
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Selenium in Peptide Chemistry.

Özge Pehlivan1, Mateusz Waliczek1, Monika Kijewska1

  • 1Faculty of Chemistry, University of Wrocław, F. Joliot-Curie 14, 50-383 Wrocław, Poland.

Molecules (Basel, Switzerland)
|April 13, 2023
PubMed
Summary

Researchers are incorporating selenium into peptides, leveraging its unique reactivity for enhanced chemical biology applications. Selenium

Keywords:
native chemical ligationphotochemical reactionsseleniumstapled peptides

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Area of Science:

  • Chemical Biology
  • Bioorganic Chemistry
  • Peptide Chemistry

Background:

  • Selenium shares electronic configuration with sulfur but exhibits higher nucleophilicity and reactivity.
  • The Se-H bond in selenocysteine (Sec) is more acidic and oxidizable than the S-H bond in cysteine (Cys).
  • These distinct properties enable selective modification and functionalization of peptides.

Purpose of the Study:

  • To explore the unique chemical properties of selenium-containing peptides.
  • To highlight the advantages of selenium incorporation over sulfur in peptide modification.
  • To review applications of selenium-modified peptides in chemical biology.

Main Methods:

  • Comparative analysis of Se-H and S-H bond properties (acidity, reactivity, oxidation).
  • Exploration of chemical modifications applied to selenium-containing peptides.
  • Review of existing applications in native chemical ligation and peptide cyclization.

Main Results:

  • Selenium incorporation enhances peptide reactivity towards electrophiles.
  • Easier Se-H bond dissociation allows for selective peptide modification.
  • Increased susceptibility of Se-H bonds to oxidation enables functional group introduction.
  • Selenium-containing peptides are valuable tools in native chemical ligation and peptide synthesis.

Conclusions:

  • Selenium-containing peptides offer unique reactivity profiles for advanced chemical biology.
  • The distinct properties of selenium provide new avenues for peptide design and functionalization.
  • Further exploration of selenium's role in peptide chemistry promises novel applications.