Issue 8, 2022

Synthesis of the l- and d-SH2 domain of the leukaemia oncogene Bcr-Abl

Abstract

The D- and L-versions of the Bcr-Abl SH2 domain (12.7 kDa) were synthesized. Key optimizations included pseudoproline incorporation, N-terminal hydrophilic tail addition and mild N-acetoxy succinimide acetylation. Their folding and activity are as for the recombinant protein. Our results will enable engineering of mirror-image monobody antagonists of the central oncoprotein Bcr-Abl.

Graphical abstract: Synthesis of the l- and d-SH2 domain of the leukaemia oncogene Bcr-Abl

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Article information

Article type
Communication
Submitted
20 Apr 2022
Accepted
01 Jul 2022
First published
06 Jul 2022
This article is Open Access
Creative Commons BY license

RSC Chem. Biol., 2022,3, 1008-1012

Synthesis of the L- and D-SH2 domain of the leukaemia oncogene Bcr-Abl

N. Schmidt, F. Abendroth, O. Vázquez and O. Hantschel, RSC Chem. Biol., 2022, 3, 1008 DOI: 10.1039/D2CB00108J

This article is licensed under a Creative Commons Attribution 3.0 Unported Licence. You can use material from this article in other publications without requesting further permissions from the RSC, provided that the correct acknowledgement is given.

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