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Journal Article

Design of protein congeners containing beta-cyclopropylalanine


Acevedo-Rocha,  Carlos G.
Research Department Reetz, Max-Planck-Institut für Kohlenforschung, Max Planck Society;
Fachbereich Chemie, Phillipps-Universität Marburg, Hans-Meerwein-Straße, 34032 Marburg, Germany ;

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Acevedo-Rocha, C. G., Geiermann, A.-S., Budisa, N., & Merkel, L. (2013). Design of protein congeners containing beta-cyclopropylalanine. Molecular BioSystems, 8(10), 2719-2723. doi:10.1039/C2MB25193K.

Cite as: https://hdl.handle.net/11858/00-001M-0000-000E-F28D-0
Abstract: The non-canonical amino acid (ncAA) analogue of methionine (Met), beta-cyclopropylalanine (Cpa), was successfully incorporated into recombinant proteins expressed in Escherichia coli in a residue-specific manner. Proteins substituted in this way are congeners because they derive from the same gene sequence as the parent protein but contain a fraction of ncAAs. We have expressed congeners using parent and mutant gene sequences of various proteins (lipase, annexin A5, enhanced green fluorescent protein, and barstar) and found that Cpa incorporation is highly dependent on the protein sequence composition. These results indicate that the global amino acid composition of proteins might be a crucial parameter that influences the outcome of unnatural translation. In addition, we could also demonstrate that the chemical nature of the second residue could be essential for successful ncAA incorporation.