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Publications 2010 - 2012

Design of protein congeners containing beta-cyclopropylalanine
Citation key 094.2012.acevedo
Author Acevedo-Rocha, C. G. and Geiermann, A. S. and Budisa, N. and Merkel, L.
Pages 2719-2723
Year 2012
DOI 10.1039/C2MB25193K
Journal Mol. BioSyst.
Volume 8
Abstract The non-canonical amino acid (ncAA) analogue of methionine (Met), β-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.
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