Abstract
Correction for ‘A simple and traceless solid phase method simplifies the assembly of large peptides and the access to challenging proteins’ by N. Ollivier et al., Chem. Sci., 2017, DOI: ; 10.1039/c7sc01912b.
The authors regret that entries 2 and 3 in Table 1 are incorrect in the original manuscript. Entry 2 is missing the CH2CH2O group and entry 3 is missing two carbonyl groups.
Table 1. Linker strategies for solid phase protein synthesis in the N-to-C direction.
| Entry | Functional linker (FL) | Attachment method for peptide segment 1 | Latent thioester (LT) |
Cleavage | Ref. | |
| Structure | Activation method | |||||
| 1 |
|
Oximation pH 4 |
|
Alkylation with bromoacetic acid, pH 4.6 | β-Elimination, aqueous base, pH 13 | 22 |
| 2 |
|
CuAAC pH 7 or SPAAC pH 2 |
|
Reduction (TCEP) and exchange by 3-mercaptopropionic acid, pH 4 | See entry 1 | 40 |
| 3 |
|
CuAAC | Note a | Transimination, 1 M H2NOH, pH 7–8.5 | 44 | |
| 4 (This work) |
|
Oximation pH 3–4 |
|
See entry 2 | Transoximation 0.025 M H2NOH, 3 M aniline, pH 3 | |
aThe method was used for the synthesis of large protein mimetics through CuAAC ligation.
A corrected version of Table 1 has been presented below:
The Royal Society of Chemistry apologises for these errors and any consequent inconvenience to authors and readers.
