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Synfacts 2022; 18(09): 1043
DOI: 10.1055/s-0041-1738552
DOI: 10.1055/s-0041-1738552
Peptide Chemistry
Synthesis of Peptides with the Formation of Highly Sterically Hindered Peptide Bonds
Wang X,
Li J,
Hayashi Y.
*
Tohoku University, Sendai, Japan
Highly Sterically Hindered Peptide Bond Formation between α,α-Disubstituted α-Amino Acids and N-Alkyl Cysteines Using α,α-Disubstituted α-Amidonitrile.
J. Am. Chem. Soc. 2022;
144: 10145-10150
DOI: 10.1021/jacs.2c02993.
Highly Sterically Hindered Peptide Bond Formation between α,α-Disubstituted α-Amino Acids and N-Alkyl Cysteines Using α,α-Disubstituted α-Amidonitrile.
J. Am. Chem. Soc. 2022;
144: 10145-10150
DOI: 10.1021/jacs.2c02993.
Significance
The introduction of unnatural amino acids, such as α,α-disubstituted α-amino acids, into peptide backbones is important in drug discovery and medicinal chemistry. The authors have developed a synthetic method for forming such highly hindered peptide bonds from α,α-disubstituted α-amidonitriles and N-alkylcysteines.
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Comment
The method produced hindered peptide bonds in good yields. The reaction of α,α-disubstituted α-amidonitriles with N-alkylcysteines proceeds in the absence of a coupling reagent.
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Publication History
Article published online:
18 August 2022
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