| Autor: |
Spears RJ; UCL Department of Chemistry, 20 Gordon Street, London WC1H 0AJ, UK. v.chudasama@ucl.ac.uk., Chrzastek A; UCL Department of Chemistry, 20 Gordon Street, London WC1H 0AJ, UK. v.chudasama@ucl.ac.uk., Yap SY; UCL Department of Chemistry, 20 Gordon Street, London WC1H 0AJ, UK. v.chudasama@ucl.ac.uk., Karu K; UCL Department of Chemistry, 20 Gordon Street, London WC1H 0AJ, UK. v.chudasama@ucl.ac.uk., Aliev AE; UCL Department of Chemistry, 20 Gordon Street, London WC1H 0AJ, UK. v.chudasama@ucl.ac.uk., Baker JR; UCL Department of Chemistry, 20 Gordon Street, London WC1H 0AJ, UK. v.chudasama@ucl.ac.uk., Chudasama V; UCL Department of Chemistry, 20 Gordon Street, London WC1H 0AJ, UK. v.chudasama@ucl.ac.uk. |
| Abstrakt: |
Herein we report a fundamental discovery on the use of tris(dialkylamino)phosphine reagents for peptide and protein modification. We discovered that C-terminal thiophosphonium species, which are uniquely stable, could be selectively and rapidly generated from their disulfide counterparts. In sharp and direct contrast, internal thiophosphonium species rapidly degrade to dehydroalanine. We demonstrate this remarkable chemoselectivity on a bis-cysteine model peptide, and the formation of a stable C-terminal-thiophosphonium adduct on an antibody fragment, as well as characterise the species in various small molecule/peptide studies. |
