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Peptide Bonds02:43

Peptide Bonds

88.0K
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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Aromatic Hydrocarbon Anions: Structural Overview01:18

Aromatic Hydrocarbon Anions: Structural Overview

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Neutral hydrocarbons like cyclopentadiene with an odd number of carbon atoms and one intervening CH2 group in the ring are not aromatic. Cyclopentadiene with 4 π electrons does not satisfy the 4n + 2 π electron rule. Additionally, the intervening CH2 group is sp3 hybridized and lacks a vacant p orbital, thereby interrupting the overlap of p orbitals in a continuous manner and preventing the delocalization of π electrons throughout the ring.
Due to the absence of continuous...
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Mass Spectrometry of Amines01:15

Mass Spectrometry of Amines

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In mass spectroscopy, amines undergo fragmentation to give parent ions with odd molecule weights. This observed mass spectrum follows the nitrogen rule; a molecule with an odd number of nitrogen atoms produces a molecular ion with an odd molecular weight. Amines undergo fragmentation through α cleavage, producing nitrogen-containing cations—iminium ions—and alkyl radicals. Mass spectra of aromatic and cyclic aliphatic amines exhibit strong molecular ion peaks, but acyclic...
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Amino acids03:42

Amino acids

112.1K
Amino acids are the monomers that comprise proteins. Each amino acid has the same fundamental structure, which consists of a central carbon atom, or the alpha (α) carbon, bonded to an amino group (NH2), a carboxyl group (COOH), and to a hydrogen atom. Every amino acid also has another atom or group of atoms bonded to the central atom known as the R group. There are 20 common amino acids present in proteins, each with a different R group. Variation in the amino acid sequence is responsible...
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Anionic Chain-Growth Polymerization: Overview01:20

Anionic Chain-Growth Polymerization: Overview

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The polymerization process that involves carbanion as an intermediate is called anionic polymerization. It is also a type of addition or chain-growth polymerization. Anionic polymerization gets initiated by a strong nucleophile such as an organolithium or a Grignard reagent. The most commonly used initiator for anionic polymerization is butyl lithium. Monomers involved in anionic polymerization must possess a vinyl group bonded to one or two electron-withdrawing groups. For instance,...
2.8K
Structure of Amines01:19

Structure of Amines

3.5K
The hybridized nitrogen atom in amines possesses a lone pair of electrons and is bound to three substituents with a bond angle of around 108°, which is less than the tetrahedral angle of 109.5°. However, the C–N–H bond angle is slightly larger at 112°, with a carbon–nitrogen bond length of 147 pm. This carbon–nitrogen bond length of of amines is longer than the carbon–oxygen bond of alcohols (143 pm) but shorter than alkanes’...
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Constructing Cyclic Peptides Using an On-Tether Sulfonium Center
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Anion recognition by cyclic peptides.

Robert B P Elmes1, Katrina A Jolliffe

  • 1School of Chemistry, The University of Sydney, 2006, NSW, Australia. kate.jolliffe@sydney.edu.au.

Chemical Communications (Cambridge, England)
|February 4, 2015
PubMed
Summary

Cyclic peptides offer precise control for designing anion receptors. This review highlights their recent applications in selectively binding various anionic species, mimicking nature's efficiency.

Area of Science:

  • Supramolecular Chemistry
  • Organic Chemistry
  • Biochemistry

Background:

  • Anion binding selectivity is crucial in chemical and biological systems.
  • Nature utilizes large peptides and proteins for efficient anion recognition.
  • Precise arrangement of recognition moieties dictates binding selectivity.

Purpose of the Study:

  • To review the recent applications of cyclic peptide scaffolds as synthetic anion receptors.
  • To highlight the advantages of cyclic peptides in controlling anion binding selectivity.
  • To showcase the versatility of cyclic peptides in mimicking natural anion binding.

Main Methods:

  • Literature review of recent studies on cyclic peptides as anion receptors.
  • Analysis of structural features of cyclic peptides enabling preorganization.

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  • Discussion of synthetic strategies for designing cyclic peptide receptors.
  • Main Results:

    • Cyclic peptides provide a rigid scaffold for preorganizing binding residues.
    • Synthetic versatility allows precise control over the size and shape of receptors.
    • Numerous examples demonstrate selective binding of various anionic species.

    Conclusions:

    • Cyclic peptides are effective and tunable scaffolds for anion receptor design.
    • They offer a synthetic route to mimic and surpass natural anion binding selectivity.
    • Further development holds promise for applications in sensing and separation.