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Published on: January 26, 2016
Efficient methodology for the cyclization of linear peptide libraries via intramolecular S-alkylation using Multipin
Kade D Roberts1, John N Lambert, Nicholas J Ede
1School of Chemistry, The University of Melbourne, Grattan Street, Parkville, Victoria 3010, Australia. kade_roberts@mimotopes.com
Summary
This study introduces an efficient method for synthesizing cyclic thioether peptides using Multipin solid phase peptide synthesis (SPPS) and S-alkylation chemistry. A 72-member library of peptide derivatives was created, targeting enzyme active sites.
Area of Science:
- Medicinal Chemistry
- Organic Synthesis
- Biochemistry
Background:
- Type II restriction endonucleases are crucial enzymes in molecular biology.
- Conserved motifs in enzyme active sites are key targets for drug discovery.
- Developing efficient synthesis methods for peptide derivatives is essential for biochemical studies.
Purpose of the Study:
- To describe an efficient parallel synthesis and cyclization methodology for peptide libraries.
- To demonstrate the utility of this method by synthesizing cyclic thioether peptide derivatives.
- To investigate structural motifs found in restriction endonuclease active sites.
Main Methods:
- Intramolecular S-alkylation chemistry.
- Multipin solid phase peptide synthesis (SPPS).
- Combinatorial library synthesis.
Main Results:
- An efficient parallel synthesis and cyclization method was established.
- A 72-member combinatorial library of cyclic thioether peptide derivatives was successfully synthesized.
- The synthesized peptides are derivatives of the DD/EXK motif found in type II restriction endonucleases.
Conclusions:
- The described methodology enables efficient parallel synthesis of cyclic peptide libraries.
- This approach is effective for creating diverse peptide derivatives for biochemical research.
- The study provides valuable peptide analogs for studying restriction endonuclease function.
