Journal
CHEMICAL COMMUNICATIONS
Volume 58, Issue 35, Pages 5359-5362Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/d2cc01090a
Keywords
-
Categories
Funding
- Leverhulme Trust [RPG-2017288, RPG-2020-010]
- EPSRC [EP/T016043/1]
Ask authors/readers for more resources
In this study, we report a significant discovery regarding the use of tris(dialkylamino)phosphine reagents in peptide and protein modification. We found that C-terminal thiophosphonium species can be selectively and rapidly generated from their disulfide counterparts, with unique stability. In contrast, internal thiophosphonium species degrade quickly. We demonstrated this chemoselectivity on a model peptide and an antibody fragment, and characterized the species in various small molecule/peptide studies.
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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available