Highly Sterically Hindered Peptide Bond Formation between α,α-Disubstituted α-Amino Acids and N-Alkyl Cysteines Using α,α-Disubstituted α-Amidonitrile
Yujiro Hayashi achieved the synthesis of extremely sterically hindered peptides.
α,α-Disubstituted α-amino acids can impart distinctive conformational and pharmacological properties when incorporated into peptides and proteins. However, the formation of peptide bonds is often challenging with these sterically hindered amino acids, and few efficient methods are known. The group of Professor Yujiro Hayashi at Tohoku University (Japan) has recently achieved a breakthrough in this area of research.
Although there is not yet evidence that such a type of extremely sterically hindered peptides has the power to change the world of peptides, the authors believe that the prospect of a near breakthrough in revealing the great potential of sterically hindered peptides will be opened by the ease of manufacturing the extremely hindered peptides described in the title article. According to Professor Hayashi “one can imagine that the study of conformation and pharmacological modification of therapeutic peptides by introduction of the highly hindered peptide moiety would be of great interest, given the growing interest in this area of research. The accomplishment of synthesizing such sterically hindered peptides is expected to open new avenues for investigating their conformation, physical, and biological properties, which may have a great impact in various research fields.”
Read the full article Highly Sterically Hindered Peptide Bond Formation between α,α-Disubstituted α-Amino Acids and N-Alkyl Cysteines Using α,α-Disubstituted α-Amidonitrile
- PDF Chemistry Catalog 2022 (PDF, 4 MB)