The d- and l-versions of the Bcr-Abl SH2 domain (12.7 kDa) were synthesized. Key optimizations included pseudoproline incorporation, -terminal hydrophilic tail addition and mild -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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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC9347351 | PMC |
| http://dx.doi.org/10.1039/d2cb00108j | DOI Listing |
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