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Congeneric bio-adhesive mussel foot proteins designed by modified prolines revealed a chiral bias in unnatural translation
Citation key 091.2012.larregola
Author Larregola, M. and Moore, S. and Budisa, N.
Pages 646-650
Year 2012
DOI 10.1016/j.bbrc.2012.04.031
Journal Biochem. Biophys. Res. Commun.
Volume 421
Number 4
Abstract Chiral bias in the unnatural translation and ‘sticky’ mussel proteins. The residue-specific in vivo incorporation of hydroxylated amino acids as well as other synthetic analogs, such as fluoroprolines, emerges as the method of choice for recombinant synthesis of Pro-rich mussel adhesive protein congeners. Chemical diversifications introduced in this way provide a general route towards bio-adhesive congeners endowed with properties not developed by natural evolution. Most importantly, we have found that the co-translational incorporation of (4R)-, and (4S)-hyroxylated and fluorinated analogs into mussel proteins presented a chiral bias: the expressed protein was only detectable in samples incubated with analogs with (4R)-substituents. Possible relationship of these stereochemical preferences for (4R)-stereoisomers in the translation to intracellular tRNA concentrations, ribosomal editing and proofreading or structural effects such as preorganization remains to be addressed in future studies. These studies will generally provide a mechanistic framework for the flexibility of the translational machinery and establish the boundaries of the unnatural translation.
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