Multi-functionalized chiral crown ethers as enzyme models for the synthesis of peptides. Multiple chiral recognition in the enzyme model

Shigeki Sasaki, Kenji Koga

Research output: Contribution to journalArticle

15 Citations (Scopus)

Abstract

A novel approach to the enzyme model for the synthesis of peptides has been established by using multi-functionalized chiral crown ethers as hosts. The new strategy consists of three key steps as follows. (1) Guest assembly: the host having one free thiol and one thioester with N-protected α-amino acid or peptide proceeds via rapid intra-complex thiolysis of α-amino acid ester salts to form the dithioester, and assembles two guests. (2) Amide formation: the intramolecular aminolysis occurs between the bound guests to form the amide bond. (3) Peptide chain elongation: as the thiol reactive group is regenerated, the above two reactions are repeated to elongate the peptide chain. In the present paper, we describe the multiple chiral recognition that could be achieved by the chiral crown ether in both the intra-complex thiolysis and the intramolecular aminolysis. For explanation of the chiral recognition, we propose a likely structure for the intermediate of the aminolysis.

Original languageEnglish
Pages (from-to)267-276
Number of pages10
JournalJournal of Inclusion Phenomena and Molecular Recognition in Chemistry
Volume7
Issue number2
DOIs
Publication statusPublished - Apr 1 1989
Externally publishedYes

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Crown Ethers
peptides
enzymes
ethers
Peptides
synthesis
Enzymes
amides
thiols
Sulfhydryl Compounds
Amides
amino acids
Amino Acids
elongation
esters
Elongation
Esters
Salts
assembly
salts

All Science Journal Classification (ASJC) codes

  • Food Science
  • Chemistry(all)
  • Condensed Matter Physics

Cite this

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abstract = "A novel approach to the enzyme model for the synthesis of peptides has been established by using multi-functionalized chiral crown ethers as hosts. The new strategy consists of three key steps as follows. (1) Guest assembly: the host having one free thiol and one thioester with N-protected α-amino acid or peptide proceeds via rapid intra-complex thiolysis of α-amino acid ester salts to form the dithioester, and assembles two guests. (2) Amide formation: the intramolecular aminolysis occurs between the bound guests to form the amide bond. (3) Peptide chain elongation: as the thiol reactive group is regenerated, the above two reactions are repeated to elongate the peptide chain. In the present paper, we describe the multiple chiral recognition that could be achieved by the chiral crown ether in both the intra-complex thiolysis and the intramolecular aminolysis. For explanation of the chiral recognition, we propose a likely structure for the intermediate of the aminolysis.",
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N2 - A novel approach to the enzyme model for the synthesis of peptides has been established by using multi-functionalized chiral crown ethers as hosts. The new strategy consists of three key steps as follows. (1) Guest assembly: the host having one free thiol and one thioester with N-protected α-amino acid or peptide proceeds via rapid intra-complex thiolysis of α-amino acid ester salts to form the dithioester, and assembles two guests. (2) Amide formation: the intramolecular aminolysis occurs between the bound guests to form the amide bond. (3) Peptide chain elongation: as the thiol reactive group is regenerated, the above two reactions are repeated to elongate the peptide chain. In the present paper, we describe the multiple chiral recognition that could be achieved by the chiral crown ether in both the intra-complex thiolysis and the intramolecular aminolysis. For explanation of the chiral recognition, we propose a likely structure for the intermediate of the aminolysis.

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