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Issue 10, 2010
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The chemical ligation of selectively S-acylated cysteine peptides to form native peptides via 5-, 11- and 14-membered cyclic transition states

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Abstract

Cysteine and C-terminal cysteine peptides are selectively S-acylated at 0–20 °C by N-(Pg-α-aminoacyl)benzotriazoles to give N-Pg-S-acyl-isodi-, -isotri-, and -isotetra-peptides isolated in good yields. N-Fmoc-S-acyl-isopeptides are Fmoc deprotected to afford free S-acyl-isopeptides isolated in high yields. S-Acyl-isodi-, S-acyl-isotetra-, and S-acyl-isopenta-peptides undergo chemical ligation; migration of the cysteine S-acyl groups to the N-terminal amino acids via 5-, 11-, and 14-membered transition states giving the corresponding native di-, tetra-, and penta-peptides. By contrast, the S-acyl-isotripeptide prefers intermolecular acylation from one molecule to another over an 8-membered intramolecular transition state. The developed methodology allows convenient isolation of stable, unprotected S-acyl cysteine peptides including the first isolation of S-acyl-isopeptides, which should facilitate the investigation of ligation by physical organic chemistry techniques.

Graphical abstract: The chemical ligation of selectively S-acylated cysteine peptides to form native peptides via 5-, 11- and 14-membered cyclic transition states

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Publication details

The article was received on 19 Feb 2010, accepted on 23 Mar 2010 and first published on 07 Apr 2010


Article type: Communication
DOI: 10.1039/C003234D
Citation: Org. Biomol. Chem., 2010,8, 2316-2319
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    The chemical ligation of selectively S-acylated cysteine peptides to form native peptides via 5-, 11- and 14-membered cyclic transition states

    A. R. Katritzky, N. E. Abo-Dya, S. R. Tala and Z. K. Abdel-Samii, Org. Biomol. Chem., 2010, 8, 2316
    DOI: 10.1039/C003234D

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