Published September 23, 2020
| Version Submitted
Journal article
Open
Serine-Selective Bioconjugation
Authors/Creators
- Vantourout, Julien C.1
- Rao Adusumalli, Srinivasa2
- Knouse, Kyle W.1
- Flood, Dillon1
- Ramirez, Antonio3
-
M. Padial, Natalia1
- Israte, Alena2
- Maziarz, Katarzyna1
- deGruyter, Justine N.4
- Merchant, Rohan R.1
- Qiao, Jennifer X.3
- Schmidt, Michael A.3
- Deery, Michael J.5
- Eastgate, Martin D.3
- Dawson, Philip E.1
- Bernardes, Gonçalo J. L.2
- Baran, Phil S.1
- 1. Department of Chemistry, Scripps Research, 10550 North Torrey Pines Road, La Jolla, CA 92037, United States.
- 2. Department of Chemistry, University of Cambridge, Lensfield Road, CB2 1EW Cambridge, United Kingdom
- 3. Chemical Process Development, Bristol-Myers Squibb, One Squibb Drive, New Brunswick, NJ 08903, United States.
- 4. 1Department of Chemistry, Scripps Research, 10550 North Torrey Pines Road, La Jolla, CA 92037, United States.
- 5. Cambridge Centre for Proteomics, Milner Therapeutics Institute, Jeffrey Cheah Biomedical Centre, University of Cambridge, Puddicombe Way, CB2 0AW Cambridge, United Kingdom
Description
The first general method for the rapid, chemoselective, and modular functionalization of serine residues in native polypeptides is reported. Using a reagent platform based on P(V) oxidation state, this redox-economic approach can be used to append nearly any kind of cargo onto serine generating a stable, benign, and hydrophilic phosphorothioate linkage. The method tolerates all other known nucleophilic functional groups of naturally occurring proteinogenic amino acids. A variety of applications can be envisaged enabled by this expansion of the toolbox of site-selective bioconjugation methods.
Files
Serine_Submitted.pdf
Files
(3.3 MB)
| Name | Size | Download all |
|---|---|---|
|
md5:2269fd2fcac8d8b866a05bbc608d5949
|
3.3 MB | Preview Download |
Additional details
Related works
- Is supplemented by
- 10.1021/jacs.0c05595 (DOI)