Prior disulfide bond-mediated Ser/Thr ligation.
| Autor: | Liu H; Department of Chemistry, State Key Laboratory of Synthetic Chemistry, The University of Hong Kong Hong Kong SAR P. R. China xuechenl@hku.hk., Chow HY; Department of Chemistry, State Key Laboratory of Synthetic Chemistry, The University of Hong Kong Hong Kong SAR P. R. China xuechenl@hku.hk., Liu J; Department of Chemistry, State Key Laboratory of Synthetic Chemistry, The University of Hong Kong Hong Kong SAR P. R. China xuechenl@hku.hk., Shi P; Department of Chemistry, State Key Laboratory of Synthetic Chemistry, The University of Hong Kong Hong Kong SAR P. R. China xuechenl@hku.hk., Li X; Department of Chemistry, State Key Laboratory of Synthetic Chemistry, The University of Hong Kong Hong Kong SAR P. R. China xuechenl@hku.hk. |
|---|---|
| Jazyk: | angličtina |
| Zdroj: | Chemical science [Chem Sci] 2024 Aug 19. Date of Electronic Publication: 2024 Aug 19. |
| DOI: | 10.1039/d4sc04825c |
| Abstrakt: | In this work, we developed a novel strategy, prior disulfide bond-mediated Ser/Thr ligation (PD-STL), for the chemical synthesis of peptides and proteins. This approach combines disulfide bond-forming chemistry with Ser/Thr ligation (STL), converting intermolecular STL into intramolecular STL to effectively proceed regardless of concentrations. We demonstrated the effectiveness of PD-STL under high dilution conditions, even for the relatively inert C-terminal proline at the ligation site. Additionally, we applied this method to synthesize the N-terminal cytoplasmic domain (2-104) of caveolin-1 and its Tyr14 phosphorylated form. Competing Interests: There are no conflicts to declare. (This journal is © The Royal Society of Chemistry.) |
| Databáze: | MEDLINE |
| Externí odkaz: |
|