# Correction: A simple and traceless solid phase method simplifies the assembly of large peptides and the access to challenging proteins

N Ollivier, R Desmet, H Drobecq, A Blanpain, E Boll, B Leclercq, A Mougel, J Vicogne, O Melnyk

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N Ollivier, R Desmet, H Drobecq, A Blanpain, E Boll, et al.. Correction: A simple and traceless solid phase method simplifies the assembly of large peptides and the access to challenging proteins. Chemical Science, 2017, 8 (8), 10.1039/c7sc90046e. hal-04751367

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Cite this: *Chem. Sci.*, 2017, **8**, 5802

DOI: 10.1039/c7sc90046e

www.rsc.org/chemicalscience

# Correction: A simple and traceless solid phase method simplifies the assembly of large peptides and the access to challenging proteins

N. Ollivier, R. Desmet, H. Drobecq, A. Blanpain, E. Boll, B. Leclercq, A. Mougel, J. Vicogne and O. Melnyk*

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.

A corrected version of Table 1 has been presented below:

<table><caption>**Table 1** Linker strategies for solid phase protein synthesis in the N-to-C direction</caption><thead><tr><th rowspan="2">Entry</th><th rowspan="2">Functional linker (FL)</th><th rowspan="2">Attachment method for peptide segment 1</th><th colspan="2">Latent thioester (LT)</th><th rowspan="2">Cleavage</th><th rowspan="2">Ref.</th></tr><tr><th>Structure</th><th>Activation method</th></tr></thead><tbody><tr><td>1</td><td><img src="image_0_0.png" alt="Chemical structure of a thioether bridge with an N-tert-butyl group at the C-3 position."></td><td>Oximation pH 4</td><td><img src="image_0_1.png" alt="Chemical structure of a thioether bridge with an S-tert-butyl group at the C-3 position."></td><td>Alkylation with bromoacetic acid, pH 4.6</td><td>β-Elimination, aqueous base, pH 13</td><td>22</td></tr><tr><td>2</td><td><img src="image_0_2.png" alt="Chemical structure of a thioether bridge with an N-tert-butyl group at the C-3 position, and an O-tert-butyl group at the C-2 position."></td><td>CuAAC pH 7 or SPAAC pH 2</td><td><img src="image_0_3.png" alt="Chemical structure of a thioether bridge with an N-tert-butyl group at the C-3 position, and an S-tert-butyl group at the C-2 position."></td><td>Reduction (TCEP) and exchange by 3-mercaptopropionic acid, pH 4</td><td>See entry 1</td><td>40</td></tr><tr><td>3</td><td><img src="image_0_4.png" alt="Chemical structure of a thioether bridge with an N-tert-butyl group at the C-3 position, and an N-tert-butyl group at the C-2 position."></td><td>CuAAC</td><td>Note<sup>a</sup></td><td></td><td>Transimination, 1 M H<sub>2</sub>NOH, pH 7-8.5</td><td>44</td></tr><tr><td>4 (This work)</td><td><img src="image_0_5.png" alt="Chemical structure of a thioether bridge with an O-tert-butyl group at the C-3 position, and an O-tert-butyl group at the C-2 position."></td><td>Oximation pH 3-4</td><td><img src="image_0_6.png" alt="Chemical structure of a thioether bridge with an N-tert-butyl group at the C-3 position, and an S-tert-butyl group at the C-2 position."></td><td>See entry 2</td><td>Transoximation 0.025 M H<sub>2</sub>NOH, 3 M aniline, pH 3</td><td></td></tr></tbody></table>

The Royal Society of Chemistry apologises for these errors and any consequent inconvenience to authors and readers.

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<footnote>a The method was used for the synthesis of large protein mimetics through CuAAC ligation.</footnote>