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Related Concept Videos

Preparation of Amides01:29

Preparation of Amides

4.1K
Amides are synthesized by treating carboxylic acids with amines in the presence of dehydrating agents like dicyclohexylcarbodiimide (DCC).
The DCC-promoted synthesis of amides begins with the protonation of DCC by carboxylic acid. The protonation makes it a better acceptor. Next, the addition of carboxylate to the protonated carbodiimide gives a reactive acylating agent.
Subsequently, the amine acts as a nucleophile that attacks the acylating agent to form a tetrahedral intermediate. In the...
4.1K
Amides to Carboxylic Acids: Hydrolysis01:28

Amides to Carboxylic Acids: Hydrolysis

4.5K
Amides can undergo either acid-catalyzed hydrolysis or base-promoted hydrolysis through a typical nucleophilic acyl substitution. Each hydrolysis requires severe conditions.
Acid-catalyzed hydrolysis:
Hydrolysis of amides under acidic conditions yields carboxylic acids. Since the reaction occurs slowly, hydrolysis requires the conditions of heat.
The mechanism begins with the protonation of the carbonyl oxygen by the acid catalyst. The protonation makes the amide carbonyl carbon more...
4.5K
Amines to Amides: Acylation of Amines01:19

Amines to Amides: Acylation of Amines

3.5K
Various carboxylic acid derivatives (such as acid chlorides, esters, and anhydrides) can be used for the acylation of amines to yield amides. The reaction requires two equivalents of amines. The first amine molecule functions as a nucleophile and attacks the carbonyl carbon to produce a tetrahedral intermediate. This is followed by the loss of the leaving group and restoration of the C=O bond.
Next, the second equivalent of amine serves as a Brønsted base and deprotonates the quaternary...
3.5K
Acid Halides to Amides: Aminolysis01:07

Acid Halides to Amides: Aminolysis

4.4K
Aminolysis is a nucleophilic acyl substitution reaction, where ammonia or amines act as nucleophiles to give the substitution product. Acid halides react with ammonia, primary amines, and secondary amines to yield primary, secondary, and tertiary amides, respectively.
In the first step of the aminolysis mechanism, the amine attacks the carbonyl carbon of the acyl chloride to form a tetrahedral intermediate. In the second step, the carbonyl group is re-formed with the elimination of a chloride...
4.4K
Amides to Amines: LiAlH4 Reduction01:20

Amides to Amines: LiAlH4 Reduction

6.3K
Amide reduction with strong reducing agents like lithium aluminum hydride proceeds through a nucleophilic acyl substitution to form amines. Primary, secondary, and tertiary amides yield primary, secondary, and tertiary amines, respectively.
Amide reduction requires two equivalents of the reducing agent, acting as a source of hydride ions. As shown in the figure, the reaction is initiated with a nucleophilic attack by the hydride ion at the carbonyl carbon to form a tetrahedral intermediate.
6.3K
Preparation of Amines: Reduction of Amides and Nitriles01:13

Preparation of Amines: Reduction of Amides and Nitriles

3.0K
Nitriles can be reduced to primary amines using reducing agents like lithium aluminum hydride or catalytic hydrogenation. The reduction introduces an amino group with an extra carbon in the skeleton. Nitriles are formed from the reaction between alkyl halides and sodium cyanide through the SN2 mechanism. Primary alkyl halides are the preferred substrates to prepare nitriles.
Amides can be reduced to primary, secondary, and tertiary amines using catalytic hydrogenation, active metals like Fe,...
3.0K

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Related Experiment Video

Updated: Feb 5, 2026

Amide Coupling Reaction for the Synthesis of Bispyridine-based Ligands and Their Complexation to Platinum as Dinuclear Anticancer Agents
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Amide Coupling Reaction for the Synthesis of Bispyridine-based Ligands and Their Complexation to Platinum as Dinuclear Anticancer Agents

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Direct amide

Alons Lends1, Francesco Ravotti1, Giorgia Zandomeneghi1

  • 1Physical Chemistry, ETH Zürich, Vladimir-Prelog-Weg 2, 8093, Zurich, Switzerland.

Journal of Biomolecular NMR
|September 13, 2018
PubMed
Summary
This summary is machine-generated.

This study introduces a selective 3D NMR experiment for protein structure analysis. It enhances signal intensity and selectivity by directly transferring polarization from nitrogen to carbons in deuterated proteins.

Keywords:
MASMagnetisation transferProteinsSolid-state NMR

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Amide Hydrogen/Deuterium Exchange & MALDI-TOF Mass Spectrometry Analysis of Pak2 Activation
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Split-and-pool Synthesis and Characterization of Peptide Tertiary Amide Library
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Split-and-pool Synthesis and Characterization of Peptide Tertiary Amide Library

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Amide Coupling Reaction for the Synthesis of Bispyridine-based Ligands and Their Complexation to Platinum as Dinuclear Anticancer Agents
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Amide Hydrogen/Deuterium Exchange & MALDI-TOF Mass Spectrometry Analysis of Pak2 Activation
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Split-and-pool Synthesis and Characterization of Peptide Tertiary Amide Library
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Split-and-pool Synthesis and Characterization of Peptide Tertiary Amide Library

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Nuclear Magnetic Resonance (NMR) Spectroscopy

Background:

  • Protein structure characterization relies on NMR chemical shift assignment.
  • Proton-detected fast Magic Angle Spinning (MAS) NMR offers new assignment avenues.
  • Existing 3D experiments suffer from low signal intensity due to inefficient polarization transfer steps.

Purpose of the Study:

  • To develop a selective 3D NMR experiment for improved protein backbone and side-chain assignment.
  • To overcome signal intensity limitations in proton-detected fast MAS NMR experiments.
  • To enhance selectivity and efficiency in polarization transfer for NMR studies.

Main Methods:

  • A selective 3D NMR experiment utilizing direct polarization transfer from backbone nitrogen to carbons.
  • Incorporation of efficient 1H-15N cross-polarization (CP) transfers, which are more efficient in deuterated proteins.
  • Employment of a dipolar INEPT experiment for nitrogen-to-carbon (N-C) transfer, avoiding less efficient HN-C and C-C CP transfers.
  • Inclusion of a selective pi pulse within the Rotational Echo Double Resonance (REDOR) transfer for targeted 13C spin polarization.

Main Results:

  • Achieved higher selectivity and increased signal intensities compared to conventional pulse sequences.
  • Demonstrated efficient polarization transfer from nitrogen to selected backbone and side-chain carbons.
  • Overcame limitations of low transfer efficiency in standard 3D sequential-assignment experiments.

Conclusions:

  • The developed selective 3D NMR experiment significantly improves signal intensity and selectivity for protein assignment.
  • This method offers a valuable tool for characterizing protein structures using NMR spectroscopy.
  • The approach is particularly effective for deuterated and amide proton back-exchanged proteins.