Enzymes, whether in their isolated form or as part of a whole cell fermentation process, have proven to be a sustainable alternative to traditional chemical catalysis for the effective conversion of natural accessible materials to high value products, such as biofuel, pharmaceuticals and agrochemicals, etc. The high enzymatic reactivity and specificity(e.g. chemo-, enantio- and regioselectivity) are however quite sensitive to enviromental conditions. Any change in the physical parameters of the aqueous media in which the enzyme has been synthsized and folded can alter its native state and consequently, enzymatic activity can be lost or seriously damaged.
Introduction of fluorinated amino acids into the hydrophobic core of enzymes imprints these biocatalysts with some outstanding properities, such as resistance to denaturation caused by organic solvents or high termperatures as a consequence of the so-called "fluorous effect" or "fluorophilicity". These chemical properties represent very valuable features for industrial applications of enzymes.
Biofluorination (also named as biological fluorination or enzymatic fluorination) means the formation process of a biological C-F bond under mild reaction conditions, biodegradability and recylability, compared traditional abiotic chemical synthesis. The fluorometabolites often show improved stability and folding as well as altered activity and fluorescence characteristics.
Nature has hardly evolved a biochemistry or enzymology of fluorine and to date only one class of enzyme has been found clearly capable of introducing the fluoride ion into an organic compound. Most of these fluorinating enzymes participate in the biosynthesis of 4-fluoro-L-threonine, the only fluorinated amino acid of natural origin discovered so far. Despite the absence of fluorometabolites in our natural product inventory and by far, a much larger challenge due to the intrinsic toxicity of the fluorometabolites and the lack of a biocatalyst capable of fluorine activation, biofluorination is a very promising and valuable tool to incorporate biofluorinated building blocks in the synthsis of peptides and proteins, using both in vivo and in vitro strategies.
Kumidas starts to explore and develop the de novo methodogies for the design and engineering of stable biofluorinated proteins and peptides for industrial and therapeutic use.
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