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