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 Experiment Videos

Enzymatic optical resolution via acylation-hydrolysis on a solid support.

Rein V Ulijn1, Nicola Bisek, Sabine L Flitsch

  • 1School of Chemistry, University of Edinburgh, King's Buildings, West Mains Road, Edinburgh, UK EH9 3JJ.

Organic & Biomolecular Chemistry
|August 22, 2003
PubMed
Summary
This summary is machine-generated.

Related Concept Videos

You might also read

Related Articles

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

Sort by
Same author

Water-Mediated Reconfigurable Topology and Mechanics in Porous Peptide Materials.

Matter·2026
Same author

Backbone-Constrained Tripeptides Enable Sequence Control of Solid-State Dynamics.

Angewandte Chemie (International ed. in English)·2026
Same author

Directed discovery of high-loading nanoaggregates enabled by drug-matched oligo-peptide excipients.

Chem·2026
Same author

Selective N-Terminal Modification of Peptides and Proteins Using Fatty Acyl Phosphates.

Angewandte Chemie (International ed. in English)·2026
Same author

Peptide Coacervates Can Protect Sequestered Oligonucleotides from Nucleases and Release Them for Transcription and Translation.

Biomacromolecules·2025
Same author

Adaptive peptide dispersions enable drying-induced biomolecule encapsulation.

Nature materials·2025
Same journal

Sulfonamides: a decade of development in synthetic methods and biological activity studies.

Organic & biomolecular chemistry·2026
Same journal

TBAF-promoted dephenolative transcarbomylation: direct access to substituted carbamates & thiocarbamates.

Organic & biomolecular chemistry·2026
Same journal

Catalytic synthesis of saturated azacycles using transborylation.

Organic & biomolecular chemistry·2026
Same journal

Pyridines with adamantane fragments and their 1,2,4-triazine analogues as anti-quorum-sensing agents, synthesis and molecular docking.

Organic & biomolecular chemistry·2026
Same journal

Synthesis of polymethylene-linked bis(cyclobutane-fused chromanones) mediated by gold photocatalysis.

Organic & biomolecular chemistry·2026
Same journal

Palladium-catalyzed chelation-assisted C-H functionalization of quinoline aldehydes to esters with mechanistic insights.

Organic & biomolecular chemistry·2026
See all related articles

This study demonstrates a novel method for producing specific dipeptide and amino acid isomers using a reversible enzyme reaction. The process efficiently yields both L,L and L,D diastereoisomers from mixed amino acid starting materials.

Area of Science:

  • Biocatalysis
  • Enzyme engineering
  • Peptide synthesis

Background:

  • Enzymatic synthesis offers a green alternative to traditional chemical peptide synthesis.
  • Thermolysin is a metalloprotease known for its ability to catalyze amide bond formation and hydrolysis.
  • Solid-phase synthesis simplifies purification and product isolation.

Purpose of the Study:

  • To develop a method for obtaining specific dipeptide and L-amino acid isomers.
  • To leverage the reversible nature of thermolysin-catalyzed reactions for stereoselective synthesis.
  • To achieve good yields of desired products from enantiomeric mixtures.

Main Methods:

  • Utilizing thermolysin immobilized on a solid support.
  • Exploiting the reversibility of the enzyme's synthesis-hydrolysis activity.

Related Experiment Videos

  • Employing enantiomeric mixtures of amino acids as starting materials.

    • Main Results:

    • Successful synthesis of L,L and L,D dipeptide diastereoisomers.
    • Efficient production of L-amino acids.
    • Good overall yields achieved for the target compounds.

    Conclusions:

    • The reversibility of thermolysin-catalyzed reactions on solid supports is a powerful tool for stereoselective peptide and amino acid synthesis.
    • This method provides a viable route to enantiomerically pure dipeptides and amino acids from racemic mixtures.
    • Solid-phase enzymatic synthesis offers an efficient and potentially scalable approach for producing valuable chiral compounds.