Abstract
The use of unnatural amino acids, particularly synthetic α-amino acids, for modern drug discovery research requires the availability of enantiomerically pure isomers. Starting from a racemate, one single enantiomer can be obtained using a deracemization process. The two more common strategies of deracemization are those obtained by stereoinversion and by dynamic kinetic resolution. Both techniques will be here described using as a substrate the d,l-3-(2-naphthyl)-alanine, a non-natural amino acid: the first one employing a multi-enzymatic redox system, the second one combining an hydrolytic enzyme together with a base-catalyzed substrate racemization. In both cases, the final product, l-3-(2-naphthyl)alanine, is recovered with good yield and excellent enantiomeric excess.
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Acknowledgements
This work was supported by Cost Action CM0701 “CASCAT, Cascade Chemoenzymatic Processes. New synergies between chemistry and biochemistry, WG2 Multistep deracemization of multifunctional compounds”.
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D’Arrigo, P., Tessaro, D. (2012). Multistep Enzyme Catalyzed Reactions for Unnatural Amino Acids. In: Pollegioni, L., Servi, S. (eds) Unnatural Amino Acids. Methods in Molecular Biology, vol 794. Humana Press. https://doi.org/10.1007/978-1-61779-331-8_2
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DOI: https://doi.org/10.1007/978-1-61779-331-8_2
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