Revisiting oxytocin through the medium of isonitriles Journal Article
| Authors: | Wang, T.; Danishefsky, S. J. |
| Article Title: | Revisiting oxytocin through the medium of isonitriles |
| Abstract: | The reaction of thioamino acids and N-terminal peptides, mediated by hindered isonitriles and hydroxybenzotriazole, gives rise to peptide bonds. In one pathway, oxytocin was synthesized by eight such reiterative amidations. In another stereospecific track, oxytocin was constructed by native chemical ligation, wherein the two building blocks were assembled by thioacid amine amidation. The NMR spectra of oxytocin and dihydrooxytocin suggest a high level of preorganization in the latter, perhaps favoring oxidative folding. © 2012 American Chemical Society. |
| Keywords: | drug synthesis; peptides; nuclear magnetic resonance spectroscopy; amino acid; molecular structure; stereospecificity; nitriles; oxidation-reduction; synthesis; isonitriles; ligation; isonitrile derivative; native chemical ligation; nmr spectrum; n-terminals; oxytocin; stereospecific; benzotriazole derivative; amidation; preorganization; oxidative folding; building blockes; hydroxybenzotriazole; peptide bonds; oxytocin derivative; thioamide |
| Journal Title: | Journal of the American Chemical Society |
| Volume: | 134 |
| Issue: | 32 |
| ISSN: | 0002-7863 |
| Publisher: | American Chemical Society |
| Date Published: | 2012-08-15 |
| Start Page: | 13244 |
| End Page: | 13247 |
| Language: | English |
| DOI: | 10.1021/ja3063452 |
| PROVIDER: | scopus |
| PMCID: | PMC3433685 |
| PUBMED: | 22830449 |
| DOI/URL: | |
| Notes: | --- - "Export Date: 4 September 2012" - "CODEN: JACSA" - "Source: Scopus" |
