Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Olefin Metathesis Polymerization: Overview01:13

Olefin Metathesis Polymerization: Overview

1.8K
Recently, the development of olefin metathesis polymerization advanced the field of polymer synthesis. Simply put, the reorganization of substituents on their double bonds between two olefins in the presence of a catalyst is known as the olefin metathesis reaction. The use of metathesis reaction for polymer synthesis is called olefin metathesis polymerization.
Ruthenium-based Grubbs catalyst is the most commonly used catalyst for olefin metathesis polymerization. Grubbs catalyst consists of a...
1.8K
Olefin Metathesis Polymerization: Acyclic Diene Metathesis (ADMET)00:53

Olefin Metathesis Polymerization: Acyclic Diene Metathesis (ADMET)

1.4K
Acyclic diene metathesis polymerization or ADMET polymerization involves cross-metathesis of terminal dienes, such as 1,8-nonadiene, to give linear unsaturated polymer and ethylene. As ADMET is a reversible process, the formed ethylene gas must be removed from the reaction mixture to complete the polymerization process.
Similar to cross-metathesis, ADMET also involves the formation of metallacyclobutane intermediate by [2+2] cycloaddition of one of the double bonds of a terminal diene with...
1.4K
Phase II Reactions: Sulfation and Conjugation with α-Amino Acids01:19

Phase II Reactions: Sulfation and Conjugation with α-Amino Acids

1.3K
Sulfation and α-amino acid conjugation are two critical biotransformation reactions in drug metabolism. Sulfation, a phase II biotransformation reaction, involves adding a polar sulfate group to a drug, enhancing its water solubility and promoting excretion. This process can either co-occur with or occur independently of glucuronidation. Nonmicrosomal sulfotransferase enzymes catalyze the process. The reaction involves 3'-phosphoadenosine-5'-phosphosulfate or PAPS coenzyme...
1.3K
Translocation of Proteins into the Mitochondria01:19

Translocation of Proteins into the Mitochondria

8.8K
Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
8.8K
Peptidoglycan Synthesis01:28

Peptidoglycan Synthesis

4.7K
Structure of PeptidoglycanPeptidoglycan is a vital structural component of the bacterial cell wall, providing mechanical strength and shape to the cell. It consists of repeating units of two sugars—N-acetylglucosamine (NAG) and N-acetylmuramic acid (NAM)—linked by β-1,4 glycosidic bonds. These sugar chains are cross-linked by short peptide chains, forming a mesh-like polymer that surrounds the bacterial plasma membrane.Cytoplasmic Phase – Precursor SynthesisPeptidoglycan...
4.7K
Acid Halides to Amides: Aminolysis01:07

Acid Halides to Amides: Aminolysis

3.7K
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...
3.7K

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Bioinspired Antimicrobial Strategy: An Extremophile Deep Sea Peptide to Combat Cystic Fibrosis Infections Caused by <i>Pseudomonas aeruginosa</i> and <i>Staphylococcus aureus</i>.

Marine drugs·2026
Same author

Cationic Permethylated Cyclodextrins Capable of Self-Assembling Into Linear Nanostructures in Water.

Chemistry (Weinheim an der Bergstrasse, Germany)·2026
Same author

Optimizing the amino terminal Cu(II)- and Ni(II)-binding (ATCUN) motif for Cu(II) complexes with improved inertness.

Chemical communications (Cambridge, England)·2026
Same author

Cosolvent Effects Question the Role of Water in Native Chemical Ligation.

Organic letters·2025
Same author

Backbone and Methyl resonance assignment of an active PETase.

Biomolecular NMR assignments·2025
Same author

Towards site-specific information on PET degrading enzymes using NMR near operational temperature.

Scientific reports·2025

Related Experiment Video

Updated: Apr 27, 2026

Imine Metathesis by Silica-Supported Catalysts Using the Methodology of Surface Organometallic Chemistry
09:37

Imine Metathesis by Silica-Supported Catalysts Using the Methodology of Surface Organometallic Chemistry

Published on: October 18, 2019

10.0K

Selenopeptide transamidation and metathesis.

Nathalie Ollivier1, Annick Blanpain, Emmanuelle Boll

  • 1CNRS UMR 8161, Institut Pasteur de Lille, Université Lille Nord de France , 59021 Lille, France.

Organic Letters
|July 15, 2014
PubMed
Summary

Mild conditions enable selenopeptide transamidation and metathesis reactions. A novel selenophosphine derived from TCEP (tris(2-carboxyethyl)phosphine) inhibits deselenization of selenocysteine residues.

More Related Videos

Author Spotlight: Advancing Structural and Biochemical Studies of Proteins Through Thermal Shift Assays
03:09

Author Spotlight: Advancing Structural and Biochemical Studies of Proteins Through Thermal Shift Assays

Published on: August 9, 2024

1.5K
Constructing Cyclic Peptides Using an On-Tether Sulfonium Center
07:11

Constructing Cyclic Peptides Using an On-Tether Sulfonium Center

Published on: September 28, 2022

2.3K

Related Experiment Videos

Last Updated: Apr 27, 2026

Imine Metathesis by Silica-Supported Catalysts Using the Methodology of Surface Organometallic Chemistry
09:37

Imine Metathesis by Silica-Supported Catalysts Using the Methodology of Surface Organometallic Chemistry

Published on: October 18, 2019

10.0K
Author Spotlight: Advancing Structural and Biochemical Studies of Proteins Through Thermal Shift Assays
03:09

Author Spotlight: Advancing Structural and Biochemical Studies of Proteins Through Thermal Shift Assays

Published on: August 9, 2024

1.5K
Constructing Cyclic Peptides Using an On-Tether Sulfonium Center
07:11

Constructing Cyclic Peptides Using an On-Tether Sulfonium Center

Published on: September 28, 2022

2.3K

Area of Science:

  • Organic Chemistry
  • Biochemistry
  • Chemical Biology

Background:

  • Selenopeptides are gaining attention as versatile biomolecules.
  • Understanding their reactivity under physiological conditions is crucial for applications.
  • Existing methods for modifying selenopeptides are limited.

Purpose of the Study:

  • To explore the reactivity of selenopeptides under mild aqueous conditions.
  • To investigate the catalytic potential of arylthiols in selenopeptide transformations.
  • To develop strategies for stabilizing selenocysteine residues.

Main Methods:

  • Transamidation reactions of selenopeptides with cysteinyl peptides in water.
  • Metathesis reactions of selenopeptides under mild catalysis.
  • Synthesis and application of a TCEP-derived selenophosphine (TCEP═Se) for inhibition studies.

Main Results:

  • Selenopeptides undergo efficient transamidation with cysteinyl peptides at pH 5.5 and 37 °C.
  • The same mild conditions also catalyze selenopeptide metathesis.
  • TCEP═Se effectively inhibits the deselenization of selenocysteine induced by TCEP.

Conclusions:

  • Mild, aqueous conditions are suitable for diverse selenopeptide modifications.
  • Arylthiol catalysis offers a new route for selenopeptide functionalization.
  • TCEP═Se represents a promising tool for protecting selenocysteine residues.